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FFFuuunnngggaaalll GGGeeennneeetttiiicccsss aaannnddd

MMMooollleeecccuuulllaaarrr BBBiiiooolllooogggyyy

第 15回糸状菌分子生物学コンファレンス

2015年 11月 19－20日

ルミエール府中（東京都府中市）

糸状菌分子生物学研究会

www.biochem.osakafu-u.ac.jp/~fmbsj/

2 1 —

−

−

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SO

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O-1 O-10 11 19 12:05 - 14:05 : (O-1, 2) (O-3, 4) (O-5~7) (O-8~10)C

12:05 O-1 terretonin Trt14

12:17 O-2 Tricholoma matsutake 1 1 2 1 1

1 , 2

12:29 O-3 Lecanicillium sp. PKS

NRPS

Minh Viet Nguyen

12:41 O-4 astellolide 1 β 2 2 2 1 1 92 CSRS

12:53 O-5 g

13:05 O-6 Binding features of ManR and ManS involved in cellulase and mannanase regulation in

Aspergillus nidulans

Nuo Li Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi

(Grad. Sch. Bioagric. Sci., Nagoya Univ.)

13:17 O-7 Cag1

13:29 O-8

β 9

13:41 O-9 AVR-Pia 1 1 1 2 3 1 1

1 , 2 3

13:53 O-10 CLA4 1 2 1 1 1 92

2 5 —

O-11 O-20 11 19 14:20 – 16:20 : (O-11~13) (O-14, 15) → (O-16, 17) (O-18~20)C

14:20 O-11

Anna Bergs1, Yuji Ishitsuka2, G. Ulrich Nienhaus2 1,3 1Dept of Microbiol, 2Inst of Applied Physics, Karlsruhe Institute of Technology (KIT), 3

14:32 O-12 9 a Cc.snf5

Cc.arp9 9 g ´ 1, 2 2 2 2 1 , 2

14:44 O-13 BiFC A. oryzae 1 1 2 3 1 1

1 2 3

14:56 O-14 GTPase CoTem1

15:08 O-15 Aspergillus nidulans poly (ADP-ribose) glycohydrolase

1 1 1 2 1 1

1 2

15:20 O-16 A. oryzae CRISPR/Cas9 1 19 19 19 29 19 1

1 92

15:32 O-17

, , ,

15:44 O-18 g Aspergillus oryzae

, , β , , ( )

15:56 O-19 CRISPR/Cas

˚

” 1, 2 2 2 β 2 2 3 2 1 2 3

2 6 —

16:08 O-20 ´

→ →

2 7 —

23 11 19 16:20 – 18:20

11 20 10:00 – 12:00

P-1 Investigation on the biosynthesis of stachybisbins from Stachybotrys bisbyi

Chang Li 1, Yudai Matsuda 1, Hao Gao 2, Xin Sheng Yao 2, Ikuro Abe 1

(1 Graduate School of Pharmaceutical Sciences, Univ. of Tokyo; 2 College of Pharmacy, Jinan Univ.)

P-2 l- 1 2 2 1 3 3 1

1 2 3

P-3 1 1 2 3 3 2

1 2 3

P-4 Emericella variecolor IFM42010

P-5 hydrophobin RolA 1 1 1 1 2 3 3 1,2

1 2 3

P-6 HypA

P-7 A. oryzae CRISPR/Cas9 1 19 19 19 29 19 1

1 92

P-8 A. oryzae 1 β 1 1 2 2 1

1 2

P-9 hydrophobin RolA-cutinase CutL1 CutL1 1, 1, 1, 1, 2, 1,2

1 , 2

2 8 —

P-10

, , , ,

P-11 Aspergillus - 1, 2, 3, 1,2

1 , 2 , 3

P-12 TILLING

, * ** *** *** ***

,* ** , ***

P-13

, , ,

P-14 hydrophobin RolA -cutinase CutL1 CutL1 1 1 1 2 1,2

1 2

P-15 α-1,3-

9 9 9 ( )

P-16 Aspergillus oryzae ”

P-17 g Aspergillus oryzae

, , β , ,

P-18 Coprinopsis cinerea 1, 1, 2, 2, 2, 3, 2

1 , 2 , 3

P-19 Coprinopsis cinerea 1 1 2 2 2 2

1 2

P-20 AmyR

2 9 —

P-21 ´

→ →

P-22 Coprinopsis cinerea

P-23 CRISPR/Cas

˚

” 1, 2 2 2 β 2 2 3 2 1 2 3

P-24

Anna Bergs1, Yuji Ishitsuka2, G. Ulrich Nienhaus2 1,3 1Dept of Microbiol, 2Inst of Applied

Physics, Karlsruhe Institute of Technology (KIT), 3

P-25 9 a Cc.snf5 Cc.arp9

9 g ´ 1, 2 2 2 2 1 , 2

P-26 A2 AoPlaA

P-27 A. oryzae 1 1 β 2 2 1 1

1 , 2

P-28 BiFC A. oryzae 1 1 2 3 1 1

1 2 3

P-29 Aspergillus oryzae AAA ATPase AipA

β ,

P-30 GTPase CoTem1

2 10 —

P-31 A. oryzae

β 1 Helge M. Dietrich1 2 3 1 1

1 2 3

P-32 Fus3

P-33 A. oryzae AoFus3 RhoGAP FipB

( )

P-34 α-1,3-

�

1 2 1 3 1 1,2

(1 2 3 )

P-35 RNA-seq

P-36

P-37 Aspergillus oryzae insulysin

, , ,

P-38

P-39 Aspergillus fumigatus 1 1 ,1 ,2 β , 2 , 2 1 , 2

P-40 Aspergillus nidulans ´ C

P-41 -1,3- • 1 2 2 β 3 1,4

1 2 3 4

P-42 A. oryzae AoAtg26

2 11 —

P-43 Aspergillus nidulans

β 1, 1, 1, β 2, 2, 2 1 , 2

P-44 Aspergillus nidulansにおけるホスファチジルセリンデカルボキシラーゼ遺伝子の機能解析

β 1 2 2 2 1 2

P-45 Aspergillus nidulans 1 2 1 β 3 3 1

1 2 3

P-46 Aspergillus nidulans poly (ADP-ribose) glycohydrolase

1 1 1 2 1 1

1 2

P-47 Aspergillus oryzae AdmA, AdmB

P-48 1 1 2 3 1, 2

1 2 3

P-49 terretonin Trt14

P-50 Aspergillus oryzae

P-51 Emericella variecolor

β

P-52 Aspergillus oryzae

β

P-53 Tricholoma matsutake 1 1 2 1 1

1 , 2

2 12 —

P-54 Lentinula edodes

P-55 Trichoderma reesei BGLII 1 1 2 1 2 1

1 2

P-56 Aspergillus nidulans GH 134 family β-1,4-

Man134A

1, 1, 1, 1, 1, 1, α 1,

1, 1, 1, 2, 1 (1 , 2 )

P-57 g NRPS-PKS

CSRS

P-58 Phanerochaete chrysosporium PQQ

1 2 1 2 1 1 1 2

P-59 Aspergillus nidulans β-D-

β

P-60 D- D-LDH

, , ( )

P-61 Aspergillus fumigatus

β

P-62 1

AtfA

β

P-63 *

P-64 ´

, ,

2 13 —

P-65

β ℃

P-66 Aspergillus terreus pH

P-67 HypD

P-68 CreA

P-69 Srs2 DNA

β 1 ” 2 3 3 1 1 1 1 2 3

P-70 Transcriptional regulation mechanism of Trichodermapepsin in Trichoderma reesei

Nayani D. Daranagama, Hiroki Aita, Hiroki Hirasawa, Koki Shioya, Haruna Sato, Yoshiyuki Suzuki, Yosuke

Shida, Wataru Ogasawara (Dept. of Bioeng., Nagaoka Univ. of Tech.)

P-71 Binding features of ManR and ManS involved in cellulase and mannanase regulation in Aspergillus

nidulans

Nuo Li Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi

(Grad. Sch. Bioagric. Sci., Nagoya Univ.)

P-72 Aspergillus oryzae PhoR

, , ,

P-73 g

P-74 XlnR

9 β 9 9 9

P-75 α- MalT

β β-

P-76 Aspergillus oryzae csrA natural antisense RNA sense RNA

2 14 —

P-77 Fusarium graminearum Tri6 5'

P-78 抗摂食性物質 citreohybridonol合成を担うシトクロム P450の発見 全智揚，松田侑大，阿部郁朗 （東大院・薬）

P-79 An unusual chimeric terpene synthase from Emericella variecolor: Diterpene synthase or sesterterpene

synthase?

Bin Qin Takahiro Mori Yudai Matsuda Masahiro Okada Takaaki Mitsuhashi Zhiyang Quan Ikuro Abe

The University of Tokyo Graduate School of Pharmaceutical Sciences

P-80 Lecanicillium sp. PKS

NRPS

, Minh Viet Nguyen, , ,

P-81 cpaM 1, 2, 2, 3, 4,5, 4, 3,

2, 2, 2 (1 , 2 , 3 , 4 , 5 )

P-82 Aspergillus kawachii 1, 2, 1, 1, 1, 3, 1, 1

1 2 3

P-83 astellolide 1 β 2 2 2 1 1 92 CSRS

P-84 1 2 1 1 2 1

1 CSRS 2

P-85 Sirtuin

P-86

β 9

P-87 g -´

2 15 —

P-88 ´ g

β 1 2 3 4 3 3

1 2 CSRS 3 4

P-89 AVR-Pia 1 1 1 2 3 1 1

1 , 2 3

P-90 Aspergillus fumigatus

β

P-91 1 2 1 1 1 1 2

P-92 ´ ´

P-93 Hope

Vy Trinh Thi Phuong

P-94 Epichloae Epichloë/Neotyphodium

1 2 3 2 1 1 1 2

P-95 26S RPN10 1 2 1 1 2

P-96 Epichloë festucae 1 1 1 1 1 Barry Scott2 3

1 1 1 2 Inst. Fund. Sci., Massey Univ. 3

P-97 Colletotrichum orbiculare species complex 9

β 1 1 2 3 Pamela Gan 4 4 2 1

1 2 3 4

2 16 —

P-98 WHI2 CoWHI2 TOR

1, 2, 1 ( 1, 2)

P-99 Aspergillus fumigatus

P-100 Aspergillus fumigatus

→ 1 2 3 2 1 2

3

P-101 CLA4 1 2 1 1 1 92

P-102 MOR

1 1 1 2 1 3 1

1 2 3

P-103

, , , , ( )

P-104 Aspergillus aculeatus

β

糸状菌分子生物学コンファレンス

第 15回記念特別シンポジウム

「糸状菌のゲノム解析・その後」

2 17 —

5 2 0 1-

4 S

Neurospora crassa 9

1843 919301940 9B. O. Dodge C. C. Lindegren 9

g 9G. W. Beadle E. L. Tatum ag 9

g 9

91950 g

9 9 19601970 g 9 1940

g g g g g 9

9Neurospora Information Conference(1)

1980 g g 9

g 9 g 1979(2)91984 RFLP (3)91986 DNA (4)91987

RIP (5)g g 919809 RFLP 9 9Fungal Genetic

Stock Center FGSC 9

9 g 9

DNA g 9DNA 9

DNA 9

1990 g 9 g 9PCR9 9

reverse genetics

9 2000 92003

2 18 —

(6)

9 g

RIP RIP 9

9RIP • 9 −

9 1 − 92004 Ninomiya(7)9 g

9 a g

KO 9 FGSC KO (8)9

KO g 9 g g g 9

g 9 9

g 9 g 9

g

1: Davis and Perkins. 2002. Nat Rev Genet 3:397-403 2: Case et al. 1979. Proc Natl Acad Sci USA 76:5259-63 3: Metzenberg et al. 1984. Neurospora Newslett 31:35-39 4: Vollmer and Yanofsky. 1986. Proc Natl Acad Sci USA 83:4869-4873 5: Selker et al. 1987. Cell 51:741-752 6: Galagan et al. 2003. Nature 422:859-868 7: Ninomiya et al. 2004. Proc Natl Acad Sci USA 101:12248-12253 8: Colot et al. 2006. Proc Natl Acad Sci U S A. 103:10352-10357 Transition of Neurospora's research method by genome analysis.

Akihiko Ichiishi

(Faculty of Life Sciences, Toyo University)

1987 1995 1997 2001 2010

2 19 —

5 2 0 1-

4 S

Aspergillus fumigatus

2003~2005 g

g Neurospora crassa Aspergillus nidulans g

g 10g g

g Aspergillus fumigatusg g g

60 A. fumigatus−g g

g − g

− g A. fumigatus

A. fumigatusa AspGD

http://www.aspgd.org g Af293, A11631439218

g g g1)

g g

g

g

− g A. fumigatusstrain-specific g

a g

g

g

A. fumigatus g

2 20 —

g −

g

g g a

g −g

9

National BioResource Project (NBRP)

g 2,3)

A. fumigatus g

g g

−

g g

− g

A. fumigatus

1: Fedorova ND, et al. PLoS Genet. 2008; 4:e1000046 2: Hagiwara D, et al. J Clin Microbiol. 2014; 52:4202-9 3: Takahashi-Nakaguchi A, et al. Med Mycol. 2015; 53:353-60 An essential role of Aspergillus fumigatus in fungal genetic biology in the next era

Daisuke Hagiwara (MMRC, Chiba Univ.)

2000 2006

COE 2007 2010 2011

2 21 —

5 2 0 1-

4 S

Aspergillus

−

9 g 9

g

a Aspergillus 91998 ´

XlnR 9a 1999AmyR 9

CreA a 1989 9

g ManR/ClrB McmA9DNA

9 a

XlnR AraR ´ XlnR ´ g DNA

A. oryzae g 75 XlnR 9 ´1) 9

XlnR A. oryzae XlnRD-´ 9 ´

9´ 9 XlnR2)

A. oryzae XlnR AraR DNA 9

AraR L- ´

9 XlnRXlnR AraR

9 9´

xdhA L- ladAXlnR AraR DNA

9 g in vitro DNAXlnR 9 DNA9AraR 9L- DNA

2 22 —

XlnR AraR XlnR g g GGCTAA

9 XlnR CGGNTAA(T/A) 8˚ 9XynF1 G2 g ´

9 GGCTAA − 9xynF1aTTAGgCTAAt 8˚ 1 9

2 XlnR 9 2−

ManR/ClrB McmA

XlnR 9 A. oryzae A. nidulans XlnR 9

−g

2012 9 a g

ManR/ClrB ManR A. oryzaeg a 3) ClrB Neurospora crassa

CLR-2 A. nidulans4) ManR ClrB 63 9

9ManR9ClrB

9A. nidulans A. oryzae g ManR/ClrB ManS9

SRF-MADS McmA5) McmA g 9A. nidulans

A eglA SRF-MADSg RNA sequencing ClrB

McmA 11 g 9

McmA ClrB

eglA eglB ClrB McmA −

9β-mannosidase mndB McmA 9

ClrB ClrB DNA McmA g DNAg 9 g g 9McmA

− a 9McmA ClrBg 9McmA a

−

g 9 g aa 9 a

2 23 —

XlnR AmyR g

9 ´

9

9

g g 9

1: Noguchi Y et al. 2009. Appl Microbiol Biotechnol 85:141-154. 2: Noguchi Y et al. 2011. Biosci Biotechnol Biochem 75:953-959. 3: Ogawa M et al. 2012. Fungal Genet Biol 49:987-995. 4: Coradetti ST et al. 2012. Proc Natl Acad Sci USA 109:7397-7402. 5: Yamakawa Y et al. 2013. Biochem Biophys Res Commun 431:777-782. Post-genomic approaches to understanding molecular mechanisms underlying regulation of

polysaccharide-degrading enzyme production in Aspergillus Tetsuo Kobayashi

(Dept of Biological Mechanisms and Functions, Grad Sch of Bioagricultural Sciences, Nagoya Univ.)

1979 1984 1984 1985 1993 1995 1999 2003

1986 -1988 1990 -1994 — —

2 24 —

5 2 0 1-

4 S

BMV 9 TMV1980 9

91997 Escherichia coli K-12˚ 9 Saccharomyces cerevisiae

9 9 19882 ( )9 7 ( 9 )

a 9 9

−g 9 -g 9

g 9 7 g

draft 13 9 14 g

g 9EST 9 g 9 9

9 9RNAi g

9 g g

9 g g

9 9 biotrophicgg 9 g 9

g CD(conditionally dispensable)9Alternaria Fusarium 9

9 9

g 9 9

g - 9

g 9 g g

g 9

g 9 9

g g 9

´ g 9

g

9 g 9

g 9 g g

2 25 —

9 g g g Genome analyses of phytopathogenic fungi and the application to plant protection

Tohru TERAOKA (Tokyo Univ. of Agric. & Techno.)

1975 1977 1977 1983 1993 1999

2 26 —

5 2 0 1-

4 S

9 9 – –

1.

9 g 9 9

9a

9 9

g 9

91980 9 9

g 9 9

9 100 9

940 9

9

g g

9 9 g 9

g

g 9 9 9

Phanerochaete chrysosporiumg 2.

P. chrysosporium a 9 197091990 9

g 9 9 P. chrysosporium g 9 9

919909 9 g

1), 2) 92004 P. chrysosporium9 9

9 a 9

9

9 9 g

2 27 —

g 9 9

g 9 9 9 Pichia pastoris3)9

9 a 4),5) 3.

9 9 9

−g 9 a

g 9 P. chrysosporium2004 JGI 6) 9 9

9 9 9

9 9

g 9

g 9 9 g

9 9 9

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g 9

9 9

9 g −g 7) 9

9 9 9

´ g8)

9JGI 9 9 1,0009) 931 a

9 9

g g 10) 4.

9 9

g 9 g

9 9 g

a g 9

9 9

9

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9 9 9

2 28 —

9 9 a

9 g g 9

−

g

1: Samejima, M., Eriksson, K.-E. L.: FEBS Lett., 292, 151-153 (1991) 2: Samejima, M., Eriksson, K.-E. L.: Eur. J. Biochem., 207, 103-107 (1992) 3: Yoshida, M. et al.: Biosci. Biotechnol. Biochem., 65, 2050-2057 (2001) 4: Igarashi, K. et al.: Biochem. J., 365, 521-526 (2002) 5: Igarashi, K. et al.: FEBS J., 272, 2869-2877 (2005) 6: Martinez, D. et al.: Nature Biotech., 22, 695-700 (2004) 7: http://www.nedo.go.jp/content/100551833.pdf 8: : 65 , p. 65, (2015) 9: http://genome.jgi.doe.gov/programs/fungi/1000fungalgenomes.jsf 10: Floudas D. et al.: Science, 336, 1715-1719 (2012) What can we think and what shall we think in the age of genomic information

– My understanding from the research on wood-decaying fungi –

Masahiro Samejima

(Department of Biomaterial Sciences, Univ. of Tokyo)

1977 1982 1982 1983 1994 1995 2001

1983 1990 -1992

�

�

�

�

Oral Session �

2 29 —

O-1 (P-49) terretonin Trt14

g gAspergillus terreus terretonin a

terretonin Trt14 ag L- [methyl-13C] methionine

Trt14 g ´1 Trt14

Trt14 His6

X Trt14˚ a Trt14

g A. oryzae NSAR1 terertonin andrastin A austinol

Trt14 gTrt14

a 1 Matsuda, Y., Iwabuchi, T., Wakimoto, T., Awakawa, T., Abe, I. J. Am. Chem. Soc., 137, 3393-3401 (2015)

Structural and functional studies on Trt14, a unique isomerase involving in the biosynthesis of terretonin

Taiki Iwabuchi, Yudai Matsuda, Takahiro Mori, Ikuro Abe

(Graduate School of Pharmaceutical Sciences, Univ. of Tokyo)

O-2 (P-53) Tricholoma matsutake

1 1 2 1 1

1 , 2

(Tricholoma matsutake)

g- - 9

a g

g g −9 9 PCR

T.matsutake NBRC30605 1 % Yeast Extract 0.5 % 30mRNA cDNA PCR

g

” ga

Expression analysis of polysaccharide hydrolyzing enzyme genes from Tricholoma matsutake.

Hiroki Onuma1, Yasuhisa Fukuta1, Mizuho Kusuda2, Takao Terashita1, Norifumi Shirasaka1

(1Grad-Sch. Agri., Kindai Univ., 2Grad-Sch. Life Env. Sci. Osaka Prefec Univ.)

2 30 —

O-3 (P-80) Lecanicillium sp. PKS

NRPS , Minh Viet Nguyen, , ,

PKS NRPS −g

Lecanicillium sp. MAFF635047 PKS NRPS ,

9 , PKS NRPS a

PKS NRPS

g ,

Lecanicillium sp. MAFF635047 PKS , NRPS 9

a HPLC ,

g , MS , NMR

9fusaristatin g

Identification of a novel hybrid compound synthesized by PKS and NRPS from Lecanicillium sp. MAFF635047

Miyuki Nakamura, Minh Viet Nguyen, Keiichi Ishido, Hiroshi Kinoshita, Takuya Nihira (ICBiotech, Osaka Univ.)

O-4 (P-83)

astellolide 1 β 2 2 2 1 1 92 CSRS

9 g 9

g g 9g 9 9

9 9 9 3 4

cclA ΔcclA 9 a9 2 a 9

14-deacetyl astellolide A (14-DAA) B (14-DAB)914-DAB

g 9astellolide9ΔcclA 9

NRPS astA ΔcclA 9ΔcclA 9 (ΔcclA ΔastA) LC-MS9ΔcclA ΔastA 914-DAA 14-DAB 9astA astellolide

g

Identification of astellolide biosynthetic gene cluster in Aspergillus oryzae.

Yasutomo Shinohara1, Makoto Kawatani2, Yushi Futamura2, Hiroyuki Osada2, Yasuji Koyama1

(1 Noda Ins. Sci. Res., 2RIKEN CSRS)

2 31 —

O-5 (P-73)

g

Aspergillus oryzae EST

enoA 3 gpdA 2 a2 a g

enoA 2ag 5,UTR

2a g

−g 5,RACE qRT-PCR enoA gpdA

− 3 15,UTR gg fbaA enoA g

− AcuK9AcuM enoA2015 fbaA

ORF AcuK AcuMAcuK AcuM a

Identification of glycolytic genes transcribed alternatively depending on carbon sources in Aspergillus oryzae

Taishi Inoue, Hiroki Toji, Mitsuru Takama, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi

(Div. Biosci. Biotechnol. Future Bioind., Grad. Sci. Agric. Sci, Univ. of Tohoku)

O-6 (P-71) Binding features of ManR and ManS involved in cellulase and mannanase regulation in Aspergillus nidulans Nuo Li Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi (Grad. Sch. Bioagric. Sci., Nagoya Univ.)

In A. nidulans, ManR regulates the expression of cellulolytic genes together with McmA by being recruited to CeRE

(Cellulose Responsive Element). Regulation of mannanase production is under control of both ManR and its paralog ManS. Cellobiose induces some mannanase genes (manB, manC, mndB) in a ManR dependent manner, while galactomannan induces a different set of mannanase genes (manC, manE, manF), for which ManS is responsible. In this report, we identified the sequence in CeRE recognized by ManR and showed the relationship between ManR and ManS in binding to some manannase genes.

Mutation analysis by EMSA on CGG/CCG that is within and close to CeRE on the promoter of endoglucanase gene, eglA and eglB, showed that CCG triplet in CeRE serves as ClrB recognition sequence. ManS could bind to the same 3 sites (CGGN8CCG) as ManR does on the promoter of mndB. However the 2nd binding site which showed the weakest binding affinity by ManR turned out to be bound most strongly by ManS among the three binding sites. In additionpromoter activity assay showed reporter gene with the 2nd binding site was induced in galactomannan, concerning that it is inactive in CMC. These findings indicates that ManR and ManS may possess opposite effect in regulating mndB under different inducers. In the case of binding to manB, manE and manF, both ManR and ManS can recognize CGGN9CC/GG, while most interestingly is when they were added together to the reaction, ManR-ManS heterodimer was formed. This result aroused our interest in investigating the roles of ManR and ManS in regulation of mannanase genes. Further study will focus on the clarification of inductive mechanism mediated by ManR and ManS, and the necessity of heterodimer formation.

This work was supported by the Program for Promotion of Basic and Applied Researches for Innovations in

Bio-oriented Industry and the Science and technology research promotion program for agriculture, forestry, fisheries

and food industry.

2 32 —

O-7 (P-63) Cag1

cap-growthless1g 9

cag1 cag1 Tup1 ga Tup1 9Cc.tupA

Tup1 9 DNA 9DNA9 Cag1

9 326 9Total RNA cDNA Cag19Yeast two hybrid 9 484000 cDNA

9 a Cag1 Interacting Protein CIP29CIP39CIP13a 9 CC1G_152879CC1G_116989CC1G_12764

PSORTII 99 Cag1

A screen to identify proteins interacting with Cag1 involved in cap growth of Coprinopsis cinerea.

Ryo Masuda, Hajime Muraguchi

(Dept. of Biotechnology, Akita Prefectural Univ.)

O-8 (P-86)

β 9

542012 9

RNA-Seq9

g

Mathematical Modeling for Mycorrhizal Infection using Biological Big Data and Combinatorial Optmization

Kazuo Ishii , Toshinori Kozaki , Tomomi Nakagawa

( Tokyo Univ. Agricul. Technol., Natl. Inst. Basic Biol.) .

2 33 —

O-9 (P-89) AVR-Pia

1 1 1 2 3 1 1 1 , 2

3

−AVR R

g AVR 1 a AVR-Pia R PiaPia 1 a RGA5-A C

Yeast two hybrid AVR-Pia 2 AVR-PiaF38AV40A AVR-Pia AVR-PiaF38AV40A

Pia 1a RGA5-A CAVR-PiaF38AV40A Pia

Δ AVR-PiaNMR AVR-Pia 6a g

g AVR AVR-Pizt Pyrenophora tricici-repentis ToxB

Structure and Function of AVR-Pia Protein of Magnaporthe oryzae

Shiho Fujiwara1, Yuya Highchi1,Yuki Satoh1, Toyoyuki Ose2, Masakatsu Kamiya3, Kozo Asano1, Teruo Sone1

(1Grad. Sch. Agriculture, 2Fac. Pharmaceutical Sci., 3Fac. Adv. Life Sci., Hokkaido Univ.)

O-10 (P-101) CLA4

1 2 1 1 1 92

− a 2 PAK

´ STE20g CLA4 , Δcla4 g, Δcla4 a

Δcla4 , ´ , Δcla4 ,

g g , , , Δcla4 FM4-64 ,

1 Spitzenkörper , Δcla4 0~2 CLA4− g , Δcla4 g

, 20 1CLA4 ,

Relationship between the CLA4 homologue and hyphal growth in Bipolaris maydis

Yuki Kitade1, Kosuke Izumitsu2, Takuya Sumita1, Chihiro Tanaka1

(1Grad. Sch. of Agriculture, Kyoto Univ., 2Sch.of Environmental Science,Univ. of Shiga Pref.)

2 34 —

O-11 (P-24) ��������������� ������������� Anna Bergs1, Yuji Ishitsuka 2, G. Ulrich Nienhaus2 1,3 1Dept of Microbiol, 2Inst of Applied Physics,

Karlsruhe Institute of Technology (KIT), 3

The highly polarized growth of filamentous fungi requires a continuous supply of proteins and lipids to the hyphal tip. This transport is managed by vesicle trafficking along the actin and microtubule cytoskeletons and their associated motor proteins. Although actin cables originating from the hyphal tip are essential for hyphal growth, and specific marker proteins to visualize the actin cables have been developed in filamentous fungi, the exact organization and dynamics of actin cables have remained elusive. Here we visualized actin through tropomyosin (TpmA) and Lifeact fused to fluorescent proteins in Aspergillus nidulans and studied actin dynamics and the interrelation of actin cables and microtubules. Comparison of TpmA and Lifeact as markers revealed that high concentrations of Lifeact affect the actin dynamics. Visualization of actin and microtubules at the same time revealed timely and spatially cooperated polymerization and depolymerisation between the two cytoskeletons. In addition, Ca2+ oscillation was visualized at hyphal tips using the Ca2+ sensor, cameleon. The frequency of this oscillation correlated with that of actin cable disassembly and microtubules reaching hyphal tips. Our results provide new insights into the molecular mechanism of ordered polarized growth regulated by actin cables and microtubules.

Cooperative polymerization between actin cables and microtubules in Aspergillus nidulans

Anna Bergs1, Yuji Ishitsuka2, G. Ulrich Nienhaus2, and Norio Takeshita1, 3

(1Dept of Microbiol, 2Inst of Applied Physics, Karlsruhe Institute of Technology (KIT), 3Faculty of Life and

Environmental Sciences, Univ. Tsukuba)

O-12 (P-25)

9 a Cc.snf5Cc.arp9 9 g ´

1, 2 2 2 2 1 , 2

Coprinopsis cinereaSWI/SNF Cc.snf5 ´

(Ando et al., 2013) 9Cc.Snf5 A´ Xba43

SWI/SNF RSCCc.arp9

Cc.snf5 g ga Cc.Snf5 a A

Cc.Arp9 A a g Nakazawa and Honda, 2015

Cc.arp9/Cc.snf5 Cc.snf5 Cc.arp9A OFF Cc.snf5 Cc.arp9 3A 4

Cc.arp9 g ´

Cc.Arp9, a putative nuclear actin-related protein, is involved in developmental regulation in Coprinopsis cinerea

Takehito Nakazawa1,2, Yuki Ando2, Takeshi Hata2, Kiyoshi Nakahori2

(1Grad. School of Agr. of Kyoto Univ., 2Grad. School of Nat. Sci. of Okayama Univ.)

2 35 —

O-13(P-28) BiFC A. oryzae

1 1 2 3 1 1 1 2 3

gAspergillus oryzae BiFC (bimolecular fluorescent complementation)

RIB40 a 1)

g A. oryzaeg BiFC

A. oryzae A. oryzae BiFC

“ BiFCg “

a “g

BiFCA. oryzae

1) 14 − p.49 (2014)

Analysis of cell fusion and incompatibility by BiFC in Aspergillus oryzae industrial strains

Tomoya Okabe1, Hidetoshi Nakamura1, Kazuhiro Iwashita2, Ikuo Fujii3, Jun-ichi Maruyama1, Katsuhiko Kitamoto1

(1Dept. of Biotechnol., The Univ. of Tokyo, 2NRIB, 3Osaka Pref. Univ.)

O-14 (P-30)

GTPase CoTem1

Rab GAP CoBub2/CoBfa1 GTPase CoTem1 G1/S

g LacO/LacI-GFPG1 S

DNA a LacI GFP LacI LacO

2 S cobub2 1S S CoBub2/CoBfa1

CoTem1 CoTem1CoTem1 G1 1 S

CoTem1CoBub2/CoBfa1 G1 S

CoTem1 S

Analyses of cell cycle using chromosome tagging system and localization of GTPase CoTem1 in Colletotrichum

orbiculare.

Fumi Fukada and Yasuyuki Kubo

(Life and Environmental Sciences, Kyoto Prefectural Univ.)

2 36 —

O-15 (P-46) Aspergillus nidulans poly (ADP-ribose) glycohydrolase

1 1 1 2 1 1 1 2

(ADP- ) (PAR) g 9PAR poly (ADP-ribose) polymerase (PARP) poly (ADP-ribose) glycohydrolase (PARG)

PARP 9 9DNA 9 9 9Aspergillus nidulans parp ortholog

1 a 9 A. nidulans 9 parg ortholog g 9 parg 9

A. nidulans parg 7 9 9 PARG 91 Mg2 PAR PAR

LC-MS/MS 9ADP- 9 fungal PARG (fPARG)

9 fparg 93 DNA 9 9fparg DNA 9PAR 9 fparg

PAR 9 fPARG PARG

Novel poly (ADP-ribose) glycohydrolase in Aspergillus nidulans.

Yuta Miyachi1, Mio Hirano1, Tatuya Yamamoto1, Naoki Takaya2,Motoyuki Shimizu1, Masashi Kato1

(1 Faculty of Agriculture, Univ. of Meijo 2 Univ. of Tukuba)

O-16 (P-7) A. oryzae CRISPR/Cas9

1 19 19 19 29 19 1 1

92

g g− a g Streptococcus Cas9

CRISPR/Cas9 gCas9 RNA DNA

CRISPR/Cas9Aspergillus oryzae

A. oryzae cas9 RNAwA yA /

−g pyrG A. oryzae niaD300 niaD˚ a wA yApyrG / −CRISPR/Cas9 A. oryzae

Development of CRISPR/Cas9 system for genome editing in Aspergillus oryzae

Takuya Katayama1, Hidetoshi Nakamura1, Yuki Tanaka1, Tomoya Okabe1, Wataru Fujii2, Katsuhiko Kitamoto1,

Jun-ichi Maruyama1 (1Dept. of Biotechnol., The Univ. of Tokyo, 2Dept. of Animal Res. Sci., The Univ. of Tokyo)

2 37 —

O-17 (P-13)

, , ,

g 99 CreA ´ CreB

9 9 creB 9creA g

1) 9− 9 9creA g

creB 99creA α-1,3- • 9Congo Red

Calucofluor white 9 creA g 9creB 9CreA CreB α-

´ 9

1) Ichinose et al., Appl. Microbiol. Biotechnol., 98, 335–343 (2014).

Polysaccharides composition of the cell wall of Aspergillus oryzae disruptants of genes involved in carbon

catablite repression

Sakurako Ichinose, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi

(Div. Biosci. Biotechnol. Future Bioind., Grad. Sci. Agric. Sci., Tohoku Univ.)

O-18 (P-17)

g Aspergillus oryzae , , β , , ( )

Aspergillus oryzae g , g

A. oryzae9 g

9 , g g (RIB40 ) ,

RIB40 g RIB40 ,

ligD − , pyrG 9 HiMe10 ( ligD, pyrG) HiMe10

3~4 , RIB40 , Trichoderma reeseiTregl3 enoA 9 Tregl3

40% , , g amyR (

), tppA ( ), pepE ( ) HiMe20 (ligD,ΔpyrG,ΔamyR,ΔpepE,ΔtppA) ,

Construction of non-mutagenized host strains in Aspergillus oryzae

Yasuhiro Kuchikata, Kana Tsuji, Yui Tonegawa, Shota Moriya, Harushi Nakajima

(Meiji Univ.)

2 38 —

O-19 (P-23) CRISPR/Cas

˚ ” 1, 2 2 2 β 2 2 3 2 1 2

3 DNA (DSB) ˚ g

˚ DSB gaa CRISPR/Cas a DSB

CRISPR/Cas gCRISPR/Cas

(36.1-100%)˚

g

Highly efficient targeted gene knock-out, knock-in and base substitution using fungal CRISPR/Cas system in the

rice blast fungus

Takayuki Arazoe1, 2, Kennosuke Miyoshi2, Tohru Yamato2, Tetsuo Ogawa2, Shuichi Ohsato2, Tsutomu Arie3, Shigeru

Kuwata2

(1Grad. Sch. Eng., Kobe Univ., 2Grad. Sch. Agric., Meiji Univ. 3Grad. Sch. Agric. Sci., Tokyo Univ. of Agric. & Tech.)

O-20 (P-21)

´ → →

N DNA(DBD) ( RD)

DBD Aspergillus nidulans a

AmyR( ) XlnR(´ ) ManR/ClrB( ) DBD RDg ´ AmyR::XlnR ´

XlnR::AmyR, ManR::AmyR, ManR::XlnR a AmyRRD g ManR::XlnR ´ g

´´ g ManR RD a

VP16 a

Chimeric transcription factors for process improvement in production of fungal polysaccharide-degrading

enzymes

Kaede Yamaguchi, Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi (Grad. Sch. Bioagric. Sci.,

Nagoya Univ.)

�

�

�

�

Poster Session �

2 39 —

P-1Investigation on the biosynthesis of stachybisbins from Stachybotrys bisbyi Chang Li 1, Yudai Matsuda 1, Hao Gao 2, Xin Sheng Yao 2, Ikuro Abe 1

(1 Graduate School of Pharmaceutical Sciences, Univ. of Tokyo; 2 College of Pharmacy, Jinan Univ.) Bisabosquals are meroterpenoids with unique ring system, which were isolated from fungi in the genus Stachybotrys.

They exhibit obvious inhibitory activities against the microsomal squalene synthase [1]. In our previous study, two new bisabosquals stachybisbins A-B have been isolated from wetland fungi Stachybotrys bisbyi [2], whose biosynthesis has attracted our attention. They were hybrid natural products possibly derived from orsellinic acid and farnesyl pyrophosphate (FPP). With an aim to clarify the biosynthetic pathways of stachybisbins and to find out clues on how to create the unique molecular scaffold, we set out to investigate the molecular basis for the biosynthesis of these compounds.

The draft genome sequencing of Stachybotrys bisbyi was performed, and we successfully found two possible biosynthetic gene clusters, which may be responsible for the biosynthesis of stachybisbins A and B. Then we proposed the possible biosynthetic pathway based on the information of the enzymes encoded by the clusters. To confirm the hypothesis, the genes were introduced one by one into Aspergillus oryzae according to the predicted pathway, and the metabolites of the transformants were analyzed by HPLC, MS, and NMR. Up to now, the functions of the first two genes of the pathway have been established on the basis of the heterologous expression method. Functional investigation of the other genes in the cluster is in progress. [1] Kazuyuki Minagawa, Shuichi Kouzuki, Kazuhide Nomura et al. Bisabosquals, novel squalene synthase inhibitors. The Journal of Antibiotics, 2001, 54 (11): 890-895.

[2] Yan Ru Bao, Guo Dong Chen, Yue Hua Wu et al. Stachybisbins A and B, the first cases of seco-bisabosquals from Stachybotrys bisbyi. Fitoterapia, 2015, 105:

151-155.

P-2 L-

1 2 2 1 3 3 1

1 2 3

Aspergillus oryzae L-g

− A. oryzae NSPlD1 lactate dehydrogenase (LDH) L- 45 g/L L-

L- L- L- 45% L- −g

L-100 g/L 10 g/L g 10%

´5 g/L

7.5 g/L TCA − gTCA ´

a

Effect of metabolic engineering on the L-lactate productivity by L-lactate producing Aspergillus oryzae.

Naoya Sasakura1, Satoshi Wakai2, Nanami Asai2, Chiaki Ogino1, Hiroko Tsutsumi3, Yoji Hata3, Akihiko Kondo1

(1Grad. Sch. Eng., Kobe Univ., 2Org. Adv. Sci. Tech., Kobe Univ., 3Res. Inst., Gekkeikan)

2 40 —

P-3

1 1 2 3 3 2

1 2 3

g −

cotransformation

g/ cotransformation

a

Designed-expression of multi-copy genes in genetically engineered Aspergillus oryzae

Satoshi Wakai1, Nanami Asai1, Chiaki Ogino2, Hiroko Tsutsumi3, Yoji Hata3, Akihiko Kondo2

(1Org. Adv. Sci. Tech., Kobe Univ., 2Grad. Sch. Eng., Kobe Univ., 3Res. Inst., Gekkeikan)

P-4

Emericella variecolor IFM42010

asteltoxin ´ F1-ATPase g

PKS ´asteltoxin

g asteltoxinPKS

E. variecolor IFM42010 BLAST 22 PKS

PKSEv460PKS asteltoxin Ev460PKS

amyB pTA-Ev460PKSAspergillus oryzae HPLC

g 2 a aa asteltoxin ´ β- β-

Ev460PKS asteltoxinPKS

a

Functional analysis of a polyketide synthase gene from Emericella variecolor IFM42010

Makoto Hashimoto, Hitomi Ichijo, Koutaro Fujiwara, Hitoshi Sugasawa, Isao Fujii

(School of Pharmacy, Iwate Med. Univ.)

2 41 —

P-5 hydrophobin RolA

1 1 1 1 2 3 3 1,2

1 2 3 Aspergillus oryzae hydrophobin RolA PBSA (Polybutylene

succinate-co-adipate) PBSA cutinase CutL1 CutL1 PBSAPBSA Hydrophobin

g hydrophobina AFM (Atomic Force Microscope)

QCM(Quarts Crystal Microbalance) SAM (Self-Assembled Monolayer) SAM g a 1-undecanethiol SAM

RolA QCM RolA AFM g pHRolA g RolA g 9 a 10-carboxy-1-decanethiol SAM 9 AFM

9 g pH RolA 9QCM RolA

a RolA

Analysis of adsorption mechanism of Aspergillus oryzae hydrophobin RolA to negatively charged surfaces.

Megumi Nagayama 1, Takumi Tanaka 1, Hiroki Tanabe 1, Kenji Uehara 1, Toru Takahashi 2 ,Toshihiko Arita 3,Takeshi

Higuchi 3 , Keietsu Abe 1,2 . ( 1 Grad. Sch. Agric. Sci., Tohoku Univ., 2 NICHe., Tohoku Univ., 3 IMRAM.,Tohoku

Univ.)

P-6 HypA

´- - g

g ag g

g Aspergillus oryzae

hypA ~D a gHypA/RolA

HypA

C HypAHypA

HypA

Analysis of the physical property change of the functional Hydrophobin HypA from Aspergillus oryzae .

Hiroki Nakano, Yasuhiro Kuchikata, Keisuke Domae, Asuka Kase, Harushi Nakajima

(Dept. of Agricultural chemistry.Univ. of Meiji)

2 42 —

P-7 (O-16) A. oryzae CRISPR/Cas9

1 19 19 19 29 19 1

1 92

g g− a g Streptococcus Cas9

CRISPR/Cas9 gCas9 RNA DNA

CRISPR/Cas9Aspergillus oryzae

A. oryzae cas9 RNAwA yA /

−g pyrG A. oryzae niaD300 niaD˚ a wA yApyrG / −CRISPR/Cas9 A. oryzae

Development of CRISPR/Cas9 system for genome editing in Aspergillus oryzae

Takuya Katayama1, Hidetoshi Nakamura1, Yuki Tanaka1, Tomoya Okabe1, Wataru Fujii2, Katsuhiko Kitamoto1,

Jun-ichi Maruyama1 (1Dept. of Biotechnol., The Univ. of Tokyo, 2Dept. of Animal Res. Sci., The Univ. of Tokyo)

P-8

A. oryzae 1 β 1 1 2 2 1

1 2

g

−g ag Aspergillus oryzae

Eucomonympha

a α- AmyBAmyB Kex2

HA-His6 Aspergillus aculeatus ß-A. oryzae Ni-NTA

HAß- a

Production of cellobiohydrolase from a symbiotic protist in the hindgut of the termite using Aspergillus oryzae

Marina Kitamoto1, Junki Kawada1, Jun-ichi Maruyama1, Masato Odagiri2, Shigeharu Moriya2, Manabu Arioka1

(1Dept. of Biotechnol., The Univ. of Tokyo, 2RIKEN)

2 43 —

P-9 hydrophobin RolA-cutinase CutL1 CutL1

1, 1, 1, 1, 2, 1,2

1 , 2

Aspergillus oryzae polybutylene succinate-co-adipate (PBSA)hydrophobin RolA, PBSA cutinase CutL1 hydrophobin

PBSA RolA CutL1 PBSA CutL1PBSA RolA CutL1 RolA H32, K34

CutL1 E31, D73, D142, D171g 1) ˚ CutL1

E31, D73, D142, D171 RolA-CutL1

CutL1 CutL1E109, D145, D203 RolA Ser E109S, D145S, D203S RolA QCM 1) Takahashi T., et al. Mol. Microbiol. 96:14-27 (2015)

Screening of fungal cutinase CutL1 amino acid residues involving in the interaction with hydrophobin RolA.

Yoonkyung Kim1, Yuki Terauchi1, Takumi Tanaka1, Kenji Uehara1, Toru Takahashi2, Keietsu Abe1,2

(1Grad. Sch. Agric. Sci., Tohoku Univ., 2NICHe., Tohoku Univ.)

P-10

, , , ,

, gAspergillus oryzae

, HypA , HypB

, a a His8 C HypB-His8

hypB , His8,

Ni2+ Ni2+

9 His8Ni2+ 40

Construction of heavy metal recovery systems using hydrophobins derived from Aspergillus oryzae

Satoshi Nakama, Shintaro Ohashi, Daiki Akaike, Ayaka Abuki, Harushi Nakajima

( Dept. of Agricultural chemistry. Univ. of Meiji )

2 44 —

P-11 Aspergillus�����������-����������������

1, 2, 3, 1,2

1 , 2 , 3

[ ] hydrophobinAspergillus oryzae hydrophobin RolA PBSA

PBSA cutinase CutL1 CutL1RolA N CutL1

RolA CutL1 CutC hydrophobin- g

Aspergillus [ ] N

hydrophobin CutL1 CE5 family esteraseCutL1 Aspergillus nidulans RodA RolA

Aspergillus RolA -CutL11) A. nidulans Cut1, Cut2 CutL1

RodA PBSA 1) Takahashi T., et al. Mol. Microbiol. 96:14-27 (2015)

Analysis of interaction between Aspergillus hydrophobin and Aspergillus cutinase

Takumi Tanaka1, Toru Takahashi2, Youhei Yamagata3, Keietsu Abe1,2

(1Grad. Sch. Agric. Sci., Tohoku Univ., 2 NICHe., Tohoku Univ., 3 Grad. Sch. Agric., Tokyo Univ. Agric. Technol.)

P-12 TILLING

g

gUV TILLING

a -EXG2

SR-1 UV 2 935 UV

UV 935 TILLING 1Mu789 1 7

˚ EXG2g

Mu789SR-1 2 4 4

Breeding of Lentinla edodes that suppressed lentinan degradation

Yuichi SAKAMOTO, Naotake KONNO*, Shiho SATO, Masashi MIZUNO**, Takahiro YAMAUCHI***, Katsumasa

Eda***, Fumikazu GOTO***

(IBRC; *Fac. of Agri., Utsunomiya Uni.; **Grad. School of Agri. Sci., Kobe Uni.; ***Hokken Co. Ltd.)

2 45 —

P-13 (O-17)

, , ,

g 99 CreA ´ CreB

9 9 creB 9creA g

1) 9− 9 9creA g

creB 99creA α-1,3- • 9Congo Red

Calucofluor white 9 creA g 9creB 9CreA CreB α-

´ 9

1) Ichinose et al., Appl. Microbiol. Biotechnol., 98, 335–343 (2014).

Polysaccharides composition of the cell wall of Aspergillus oryzae disruptants of genes involved in carbon

catablite repression

Sakurako Ichinose, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi

(Div. Biosci. Biotechnol. Future Bioind., Grad. Sci. Agric. Sci., Tohoku Univ.)

P-14

hydrophobin RolA -cutinase CutL1 CutL1

1 1 1 2 1,2 1 2 hydrophobin

PBSA (Polybutylene succinate-co-adipate) Aspergillus oryzae hydrophobin RolA PBSA CutL1 RolA PBSA

CutL1 PBSA CutL1 PBSA RolA N H32, K34 CutL1 E31, D142, D171

1) NaCl RolA -CutL1 NaCl RolA H32S/K34S -CutL1 (E31S/D142S/D171S)

CutL1 D30, D34, D73, D117 D73 g

g D30, D34,D117 CutL1- D30S,D34S,D117S RolA a

1) Takahashi T., et al. Mol. Microbiol. 96:14-27 (2015)

Analysis of CutL1 amino acid residues involving in interaction between Aspergillus oryzae hydrophobin RolA

and cutinase CutL1

Yuki Terauchi1, Yoonkyung Kim 1, Takumi Tanaka1, Yusei Tsushima1, Kenji Uehara1, Toru Takahashi2, Keietsu Abe1, 2

(1 Grad. Sch. Agric. Sci. Tohoku Univ., 2 NICHe Tohoku Univ.)

2 46 —

P-15 α-1,3-

9 9 9 ( )

Taka-amylase (TAA) 9

α-1,3- AGa AG (agsA,agsB,agsC) g

Cre/loxP 9 g 9agsBg TAA

9ΔagsB TAA g9AG agsB 9AG TAA

( 92014) agsB AG - PamyB

TTA 9agsA WT 9TAA 9agsA

agsB 9agsB agaC • 9 g 9PamyB

PactA ags 9TTA a

9 13 − 9p.43

Alpha-1,3-Glucan is involved in Taka-amylase adsorption on the Aspergillus oryzae cell wall in liquid culture Silai Zhang, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi

P-16 Aspergillus oryzae ”

gCoA

9.2g −g

CoA g

gg

gg

80%

High Efficient Secretion of Free Fatty Acids from Aspergillus oryzae by Supplementation of Non-Ionic

Surfactants to the Culture Medium

Koichi Tamano, Ai Miura, Hideaki Koike, Yasushi Kamisaka, Kazuyoshi Kimura, Myco Umemura, Masayuki Machida

(AIST)

2 47 —

P-17 (O-18) g Aspergillus oryzae , , β , , ( )

Aspergillus oryzae g , g

A. oryzae9 g

9 , g g (RIB40 ) ,

RIB40 g RIB40 ,

ligD − , pyrG 9 HiMe10 ( ligD, pyrG) HiMe10

3~4 , RIB40 , Trichoderma reeseiTregl3 enoA 9 Tregl3

40% , , g amyR (

), tppA ( ), pepE ( ) HiMe20 (ligD,ΔpyrG,ΔamyR,ΔpepE,ΔtppA) ,

Construction of non-mutagenized host strains in Aspergillus oryzae

Yasuhiro Kuchikata, Kana Tsuji, Yui Tonegawa, Shota Moriya, Harushi Nakajima

(Meiji Univ.) P-18 Coprinopsis cinerea

1, 1, 2, 2, 2, 3, 2 1 , 2 , 3

Coprinopsis cinerea g

g − gg g

a g

0.5M Sorbitol + 10% DMSO -806 3g g a GFP

gLuciferase assay

C.cinerea Luciferase(ffLuc) β-glucuronidase g(Collins et al. 2010) Luciferase(reLuc) ´ Luciferase(nanoLuc) a

Luciferase assay nanoLuc nanoLuc C.cinerea RNAseqA.bisporous

gpd2 10g

Development of protoplasts’ cryopreservation and its application to the promoter analyses in Coprinopsis

cinerea.

Hiroko Suzuki1, Hirofumi Chiba1, Kiyomi Okahisa2, Shigeo S Sugano2, Yuriko Osakabe2, Hajime Muraguchi3, Keishi

Osakabe2 (1Life Tech., Tokushima Univ.,2 CCAIC, Tokushima Univ., 3Biotech., Akita Pref Univ.)

2 48 —

P-19 Coprinopsis cinerea

1 1 2 2 2 2

1 2

´

g RNA

g g g RNAg Coprinopsis

cinerea #326 C.cinerea 3 µg GFP

buffer g g300 MgCl2

900 V Tris-HCl (pH 7.5), 25 mM CaCl2 (STC buffer)24 DNA 3~10%

GFP2 GFP g g GFP

48GFP

Development of the electroporation method for a model mushroom Coprinopsis cinerea

Hirofumi Chiba1, Hiroko Suzuki1, Kiyomi Okahisa2, Sigeo S Sugano2, Yuriko Osakabe2, Keishi Osakabe2

(1Life Tech., Tokushima Univ., 2CCAIC, Tokushima Univ.) P-20

AmyR

AmyR AmyR

AmyR (CreA)

(1) 0.1% ” AmyR

− ” AmyR − a0.1% ” 20

45 ”0.3 µM AmyR

0.3 µM 3 mMAmyR

g ” AmyR a

(1) Suzuki et al ., Appl Microbiol Biotechnol. 99: 1805-1815 (2015)

Intracellular localization of AmyR involved in amylase gene expression of Aspergillus oryzae in the presence of

various carbon sources

Yui Konno, Kuta Suzuki, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi

(Div.Biosci.Biotechnol.Future Bioind., Grad.Sch.Agric.Sci.,Tohoku Univ.)

2 49 —

P-21 (O-20) ´

→ →

N DNA(DBD) ( RD)

DBD Aspergillus nidulans a

AmyR( ) XlnR(´ ) ManR/ClrB( ) DBD RDg ´ AmyR::XlnR ´

XlnR::AmyR, ManR::AmyR, ManR::XlnR a AmyRRD g ManR::XlnR ´ g

´´ g ManR RD a

VP16 a

Chimeric transcription factors for process improvement in production of fungal polysaccharide-degrading

enzymes

Kaede Yamaguchi, Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi (Grad. Sch. Bioagric. Sci.,

Nagoya Univ.) P-22

Coprinopsis cinerea 1

g − a

g Coprinopsis cinerea PEG GFP C.cinerea ―

Bio-Rad S3e 8 µL/min GFPg

30 5x104 GFP MYG1/103 GFP

GFPPEG GFP g GFP

g g

aa

Exploring application of cell sorting analyses of Coprinopsis cinerea

Shigeo S Sugano, Hiroko Suzuki, Hirofumi Chiba, Yuriko Osakabe, and Keishi Osakabe

(CCAIC, Tokushima Univ., Life Tech., Tokushima Univ.)

2 50 —

P-23 (O-19) CRISPR/Cas

˚ ” 1, 2 2 2 β 2 2 3 2 1 2

3 DNA (DSB) ˚ g

˚ DSB gaa CRISPR/Cas a DSB

CRISPR/Cas gCRISPR/Cas

(36.1-100%)˚

g

Highly efficient targeted gene knock-out, knock-in and base substitution using fungal CRISPR/Cas system in the

rice blast fungus

Takayuki Arazoe1, 2, Kennosuke Miyoshi2, Tohru Yamato2, Tetsuo Ogawa2, Shuichi Ohsato2, Tsutomu Arie3, Shigeru

Kuwata2

(1Grad. Sch. Eng., Kobe Univ., 2Grad. Sch. Agric., Meiji Univ. 3Grad. Sch. Agric. Sci., Tokyo Univ. of Agric. & Tech.)

P-24 (O-11)

Anna Bergs1, Yuji Ishitsuka2, G. Ulrich Nienhaus2 1,3 1Dept of Microbiol, 2Inst of Applied Physics,

Karlsruhe Institute of Technology (KIT), 3

The highly polarized growth of filamentous fungi requires a continuous supply of proteins and lipids to the hyphal tip. This transport is managed by vesicle trafficking along the actin and microtubule cytoskeletons and their associated motor proteins. Although actin cables originating from the hyphal tip are essential for hyphal growth, and specific marker proteins to visualize the actin cables have been developed in filamentous fungi, the exact organization and dynamics of actin cables have remained elusive. Here we visualized actin through tropomyosin (TpmA) and Lifeact fused to fluorescent proteins in Aspergillus nidulans and studied actin dynamics and the interrelation of actin cables and microtubules. Comparison of TpmA and Lifeact as markers revealed that high concentrations of Lifeact affect the actin dynamics. Visualization of actin and microtubules at the same time revealed timely and spatially cooperated polymerization and depolymerisation between the two cytoskeletons. In addition, Ca2+ oscillation was visualized at hyphal tips using the Ca2+ sensor, cameleon. The frequency of this oscillation correlated with that of actin cable disassembly and microtubules reaching hyphal tips. Our results provide new insights into the molecular mechanism of ordered polarized growth regulated by actin cables and microtubules.

Cooperative polymerization between actin cables and microtubules in Aspergillus nidulans

Anna Bergs1, Yuji Ishitsuka2, G. Ulrich Nienhaus2, and Norio Takeshita1,3

(1Dept of Microbiol, 2Inst of Applied Physics, Karlsruhe Institute of Technology (KIT), 3Faculty of Life and

Environmental Sciences, Univ. Tsukuba)

2 51 —

P-25 (O-12) 9 a Cc.snf5

Cc.arp9 9 g ´ 1, 2 2 2 2 1 , 2

Coprinopsis cinerea

SWI/SNF Cc.snf5 ´ (Ando et al., 2013) 9Cc.Snf5 A

´ Xba43SWI/SNF RSC

Cc.arp9Cc.snf5 g g

a Cc.Snf5 a ACc.Arp9 A a g

Nakazawa and Honda, 2015Cc.arp9/Cc.snf5 Cc.snf5 Cc.arp9

A OFF Cc.snf5 Cc.arp9 3A 4

Cc.arp9 g ´

Cc.Arp9, a putative nuclear actin-related protein, is involved in developmental regulation in Coprinopsis cinerea

Takehito Nakazawa1,2, Yuki Ando2, Takeshi Hata2, Kiyoshi Nakahori2

(1Grad. School of Agr. of Kyoto Univ., 2Grad. School of Nat. Sci. of Okayama Univ.) P-26

A2 AoPlaA

sn-2 1-

A2 (PLA2) PLA2 (cPLA2) ´

Aspergillus oryzae cPLA2 40%cPLA2 AoplaA

AoPlaA cPLA2 cPLA2 a Ca2+

C2 cPLA2 gAoPlaA N

AoplaA PE • g PE •g AoPlaA

AoPlaA (PE) 1- PE

g gS266A AoplaA

156 S266Ag AoPlaA

AoPlaA PE

Functional analysis of mitochondria-localized phospholipase A2 AoPlaA in Aspergillus oryzae

Sho Izawa, Ayumi Takayanagi, Noriyuki Komai, Katsuhiko Kitamoto, Manabu Arioka

(Dept. of Biotechnol., Univ. of Tokyo)

2 52 —

P-27 A. oryzae

1 1 β 2 2 1 1

1 , 2

Aspergillus flavusgg

Aspergillus oryzae a g a RIB40g A.

oryzae basic helix-loop-helix SclR EcdRg g

A. oryzae A. oryzae RIB40 400

• 50SclR 50

EcdR A. oryzae

a

Screening for transcription factors involved in sclerotia formation of A. oryzae

Hidetoshi Nakamura1, Jun-ichi Maruyama1, Masahiro Ogawa2, Yasuji Koyama2, Manabu Arioka1, Katsuhiko Kitamoto1

(1Dept. of Biotechnol., The Univ. of Tokyo, 2Noda Inst. Sci. Res.) P-28 (O-13) BiFC A. oryzae

1 1 2 3 1 1 1 2 3

gAspergillus oryzae BiFC (bimolecular fluorescent complementation)

RIB40 a 1)

g A. oryzaeg BiFC

A. oryzae A. oryzae BiFC

“ BiFCg “

a “g

BiFCA. oryzae

1) 14 − p.49 (2014)

Analysis of cell fusion and incompatibility by BiFC in Aspergillus oryzae industrial strains

Tomoya Okabe1, Hidetoshi Nakamura1, Kazuhiro Iwashita2, Ikuo Fujii3, Jun-ichi Maruyama1, Katsuhiko Kitamoto1

(1Dept. of Biotechnol., The Univ. of Tokyo, 2NRIB, 3Osaka Pref. Univ.)

2 53 —

P-29 Aspergillus oryzae AAA ATPase AipA

β ,

,

, Aspergillus oryzae gg g , AoAbp1

AipA 1) AipA AAA ATPase , g , AipA bait , cDNA prey , yeast

two-hybrid (YTH) , a, g , AipA Sap1p

Yta6p , Las17p − Pil1pYTH , AoLas17, AoPil1 AipA ,

AoPil1 AipA , , AoPil1-EGFPEGFP-AipA , , AipA

AoPil1 AipA, AoPil1 , , AipA

1) Higuchi et al. (2011) FEMS Microbiol Lett 320, 63-71.

Analysis of interacting proteins with the endocytosis-associated AAA ATPase AipA in Aspergillus oryzae

Ken-ichi Kakimoto, Kaoru Takegawa, Yujiro Higuchi

(Dept. of Biosci. Biotechnol., Kyushu Univ.)

P-30 (O-14)

GTPase CoTem1

Rab GAP CoBub2/CoBfa1 GTPase CoTem1 G1/S

g LacO/LacI-GFPG1 S

DNA a LacI GFP LacI LacO

2 S cobub2 1S S CoBub2/CoBfa1

CoTem1 CoTem1CoTem1 G1 1 S

CoTem1CoBub2/CoBfa1 G1 S

CoTem1 S

Analyses of cell cycle using chromosome tagging system and localization of GTPase CoTem1 in Colletotrichum

orbiculare.

Fumi Fukada and Yasuyuki Kubo

(Life and Environmental Sciences, Kyoto Prefectural Univ.)

2 54 —

P-31 A. oryzae

β 1 Helge M. Dietrich1 2 3 1 1

1 2 3

Aspergillus oryzaeg A. oryzae AoLreA −

aAspergillus flavus A. oryzae

ag A. oryzae

A. oryzae

AolreAA. nidulans LreB LreA

A. oryzae g AoLreBAolreB AolreA

A. oryzae AoLreA AoLreB −

Functional analysis of light-response related genes in conidiation and sclerotia formation of Aspergillus oryzae

Junki Kawada1, Helge M. Dietrich1, Taisuke Watanabe2, Hirohide Toyama3, Jun-ichi Maruyama1, Katsuhiko Kitamoto1

(1Dept. of Biotechnol., The Univ. of Tokyo, 2 Dept. Biores. Util. Sci., Grad. Sch. Biores. Sci., Nihon Univ., 3Dept. of

Biosci. Biotech., Fac. of Agr., Univ. of Ryukyus)

P-32

Fus3

Saccharomyces cerevisiae mitogen-activated

protein´ Fus3p Ste12pg

Aspergillus oryzae FUS3 (Aofus3) g 1) TAPAoFus3 Ste12p

AoSte12 FipC (Fus3-Interacting Protein C) FipCg Fus3

A. oryzae AoFus3 FipC AoSte12 a

Yeast two hybrid AoFus3 FipC AoSte12 a

fipC Aoste12 /− −

Aoste12 1/3 fipC 1/60 FipCEGFP A. oryzae

AoFus3 FipC AoSte12 1) Tsukasaki et al. (2014) Biosci. Biotechnol. Biochem. 78:1254–62

Regulation mechanism of cell fusion by Fus3 ortholog and its interacting proteins in filamentous fungi

Takuya Katayama, Jun-ichi Maruyama (Dept. of Biotechnol., The Univ. of Tokyo)

2 55 —

P-33 A. oryzae AoFus3 RhoGAP FipB

( )

Aspergillus oryzae g

g Woronin bodya g MAP ´ a AoFus3

FipBFipB Rho GTPase GDP RhoGAP (Rho GTPase activating protein)a FipB g Rho GTPase

a RhoGAP FipB AoCdc42 AoRac1RhoGAP FipB AoCdc42

AoRac1 g AoCdc42 AoRac1g g fipB

Aofus3 AoCdc42 g FipB RhoGAPAoCdc42 fipB

A. oryzae FipB AoCdc42 RhoGAP AoFus3

Investigation of target GTPase of FipB, a RhoGAP protein interacting with AoFus3, in A. oryzae

Kengo Harata, Daiki Yahagi, Jun-ichi Maruyama, Katsuhiko Kitamoto

(Dept. of Biotechnol., The Univ. of Tokyo)

P-34

α-1,3-

1 2 1 3 1 1,2 (1 2

3 )

9 gg Aspergillus nidulans α-1,3-AGS agsB (ΔagsB) 9 1) 9 A. oryzae

AGS (ΔagsAΔagsBΔagsC) 9 g g9A. nidulans 9agsB a α- (agtA, amyG)

2)9 amyG agtA, amyG 99 9 AGS9agtA, amyG (ΔagsAΔagsBΔagsCΔagtAΔamyG) 9

9 9g 9 g 9agtA, amyG g 9

a 1) Yoshimi A., et al., PloS ONE 8(1):e54893 (2013), 2) He X., et al., Mol. Microbiol., 91(3):579-595 (2014)

Growth characteristics and protein production of Aspergillus oryzae quintuple disrupants of the

α-1,3-glucan-related genes under liquid culture conditions.

Ken Miyazawa1, Akira Yoshimi2, Silai Zhang1, Motoaki Sano3, Katsuya Gomi1, Keietsu Abe1,2 (1Grad. Sch. Agric. Sci.,

Tohoku Univ, 2NICHe, Tohoku Univ., 3Kanazawa Inst. Tech.)

2 56 —

P-35 RNA-seq

gRNA-seq

gg g Augustus

Ab initio gAugustus g

UTRg g a g

RNA-seqa g a

High accuracy methods for fungal genome annotation using RNA-seq

Hidenori Yamagishi, Yasuo Uemura

(Genaris Omics, Inc.)

P-36

gMoCV1-A Magnaporthe oryzae chrysovirus 1 strain A ORF4 812 aa

TDH3pro 2µoriOD600 ,

a MoCV1-B MoCV1-A 92 ORF4 89MoCV1-B , , g MoCV1-B ORF4

811 aa a MoCV1-B ORF4g g 9

GAL1pro 2µori MoCV1-B ORF4 MoCV1-B ORF4 MoCV1-B ORF4

g 5 1 g gg MoCV1-A

ORF , MoCV1-A ORF a

Evaluation of Antifungal activity in Proteins encoded by Mycoviruses using Yeast inducible promoter expression

system

Shunji Tsukimoto, Yuri Kimura, Shun Ichinose, Toshiyuki Fukuhara, Hiromitsu Moriyama (Div. of Bioregulation and

Biointeraction, Tokyo Univ. of Agriculture and Technology)

2 57 —

P-37 Aspergillus oryzae insulysin

, , ,

Aspergillus oryzae EST insulysin ortholog 3 a

Saccharomyces cerevisiae ortholog, Ste23 -prohormone , insulysin 9

Schizosaccharomyces pombe ortholog, Iph1 iph1 ER A. oryzae 3a ortholog a

g insA, insB, insC 9

A. oryzae RIB40 pyrG ligD , pyrG insA, insB, insC

insB insC a, Czapek-Dox insC • ER stressor

” Czapek-Dox 9 • 9insB insC • 9 insB

insC Czapek-Dox • , A. oryzae InsB InsC S. pombe Iph1 ER

Analysis on Physiological functions of insulysins in Aspergillus oryzae.

Haruka Suzuki, Ryohei Yoshinaga, Michio Takeuchi, Youhei Yamagata

Dept. of Applied Biological Science, Tokyo Univ. of Agriculture and Technology

P-38

/

Aspergillus oryzae

A. oryzae a A. oryzae g

g A. oryzae

Cleavage assay H2B-EGFP

AoAtg8 yeast two-hybrid 5

Aoatg11,Aoatg26

Analysis of nucleophagy, degradation of nucleus by autophagy, in Aspergillus oryzae

Takahiro MITANI, Takashi KIKUMA, Katsuhiko KITAMOTO

(Dept. of Biotechnol., Univ. of Tokyo)

2 58 —

P-39

Aspergillus fumigatus 1 1 ,1 ,2 β , 2 , 2 1 , 2

Galf 9 Aspergillus fumigatusAfGfsA O- Galf 9A.

fumigatus AfgfsA 7a 9 AfgfsB- AfgfsH AfgfsA- AfgfsH a 9 2a

g 9AfgfsA GT31-A9 GT31-BGT31-B 5a 9AfGfsA g a Galf

9A. fumigatus GT31-B A. fumigatus GT31-B 5a AfgfsD- AfgfsH a

MM 937 C9 g ” 9 960 µg/mL

(CFW) 42 C 9∆AfgfsD ∆AfgfsEg 9AfgfsD AfgfsE

CFW AfgfsD AfgfsE 50.9% a 99AfgfsD AfgfsE 2

9CFW 9AfgfsD AfgfsE 9AfGfsD AfGfsE 9

Functional analysis of the putative galactofuranosyltransferase genes in Aspergillus fumigatus 1Qiushi Li, 1Yukako Katafuchi, 1Keisuke Ekino,2Kaoru Takegawa,2Masatoshi Goto,1Takuji Oka

(1Grad. Sch. Eng., Sojo Univ.,2Fac. Agric., Kyushu Univ.)

P-40 Aspergillus nidulans ´ C

Aspergillus nidulans ´ C PkcA

g g a

g pkcA PkcACa2+ CZD mRNA

Ca2+ CrzA PkcAcell wall integrity PkcA

MAP´ MpkA (1) Saccharomyces cerevisiae CrzA Crz1

CrzA a PkcACrzA g ― PkcA

CrzA g g PkcACrzA CZD

PkcA Ca2+ a

(1) 14 − p. 55 (2014)

Activation of Ca2+ signaling pathway by pkcA-inactivation in Aspergillus nidulans

Yuki Yamamoto, Takuya Katayama, Hiroyuki Horiuchi (Dept. of Biotechnol., Univ. of Tokyo)

2 59 —

P-41

-1,3- • 1 2 2 β 3 1,4 1 2 3

4

, Aspergillus nidulans -1,3- AGAG AG CR

- BG CR BGCR BG

AG • BGg

AG CR , AG •

CR AG CRAG CR

CR , AG •

AG • a CR , CRg AG , 3

AG • g AG •

, a

Screening method for isolation of the cell wall -1,3-glucan-deficient mutants in Aspergillus oryzae.

Akira Yoshimi1, Misa Hirama2, Yasunobu Tsubota2, Kazuyoshi Kawakami3, Keietsu Abe1,4

(1NICHe, Tohoku Univ., 2Ichinokura Co., Ltd., 3Tohoku Univ. Sch. of Med., 4Grad. Sch. Agric. Sci. Tohoku Univ.)

P-42 A. oryzae AoAtg26

Aspergillus oryzae AoAtg26´

Pichia pastoris PpAtg26 ´Saccharomyces cerevisiae Atg26 g

Atg26 AoAtg26g

Aoatg26 A. oryzaeg Aoatg26 AoAtg26 AoAtg26FL

C AoAtg26 AoAtg26 CAoAtg26FL AoAtg26 C

g AoAtg26− Magnaporthe oryzae MoAtg8

Aoatg26 AoAtg8 PEAoAtg8-PE EGFP-AoAtg26F EGFP-AoAtg26 CAoatg26

Localization and functional analysis of autophagy-related protein AoAtg26 in Aspergillus oryzae

Takashi Kikuma, Manabu Arioka, Katsuhiko Kitamoto

(Dept. of Biotechnol., The Univ. of Tokyo)

2 60 —

P-43 Aspergillus nidulans

β 1, 1, 1, β 2, 2, 2 1 , 2

Aspergillus nidulans 92 9

99 rcfA 9 a

9 rcfA 405 g 9

(SOSUI) 3 AnRcfA 9 N-−g DXD 9 GnT-IVb

25% ΔrcfA 936% • 9ΔrcfA1 RcfA BLAST

36%930% 9 rcfB9rcfC 99 g g 9ΔrcfA ´

(20 µg/mL) RcfA g−g 9 g RcfA 1

9RcfA −g

Functional analysis of the putative galactofuranosyltransferase genes in Aspergillus fumigatus 1Yohei Kawamitsu, 1Chihiro Ishii, 1Keisuke Ekino, 2Kaoru Takegawa, 2Masatoshi Goto, 1Takuji Oka

(1Grad. Sch. Eng., Sojo Univ., 2Fac. Agric., Kyushu Univ.)

P-44 Aspergillus nidulansにおけるホスファチジルセリンデカルボキシラーゼ遺伝子の機能解析 β 1 2 2 2 1 2

−g a ´ C PKCPKC g

a g Aspergillus nidulans PKC pkcA PkcA

mRNA g Saccharomyces cerevisiae´ PSD) PSD2 PSD

PtdEtn 9S. cerevisiae

PKC

A. niduulans S. cerevisiae Psd2p9 3 a AN3188 AN7989 AN11161 a

ΔAN7989 ΔAN11161 g g ΔAN318825oC

9PtdEtn ” g 9ΔAN3188 ag

Functional analyses of phosphatidylserine decarboxylase-encoding genes in Aspergillus nidulans.

Akari Kikkawa1, Keiko Takagi2, Ryoichi Fukuda2, Hiroyuki Horiuchi2

(1Fac. of Agr., 2Dept. of Biotechnol., Univ. of Tokyo)

2 61 —

P-45 Aspergillus nidulans

1 2 1 β 3 3 1 1 2

3

Aspergillus nidulans Galf GfsA 99UDP-Galf O- Galf Galf g

2a g 9GfsA27.5 26.0 GfsB GfsC9Gfs g a GfsB GfsC 9

9Galf GfsB GfsC GfsAg 9ΔgfsA gfsB gfsC 9

gfsA g 9GfsB GfsC GfsAg 9RNA-Seq gfsA

9 g g9 22 GfsA ΔgfsA 9

−g

Functional analysis of galactofuranose transferases in Aspergillus nidulans

Yukako Katafuchi1 Minoru Izumi2 Keisuke Ekino1 Kaoru Takegawa3 Masatoshi Goto3 Takuji Oka1 1Univ. of

Sojo 2Univ. of Okayama 3Univ. of Kyusyu

P-46 (O-15)

Aspergillus nidulans poly (ADP-ribose) glycohydrolase

1 1 1 2 1 1 1 2

(ADP- ) (PAR) g 9PAR poly (ADP-ribose) polymerase (PARP) poly (ADP-ribose) glycohydrolase (PARG)

PARP 9 9DNA 9 9 9Aspergillus nidulans parp ortholog

1 a 9 A. nidulans 9 parg ortholog g 9 parg 9

A. nidulans parg 7 9 9 PARG 91 Mg2 PAR PAR

LC-MS/MS 9ADP- 9 fungal PARG (fPARG)

9 fparg 93 DNA 9 9fparg DNA 9PAR 9 fparg

PAR 9 fPARG PARG

Novel poly (ADP-ribose) glycohydrolase in Aspergillus nidulans.

Yuta Miyachi1, Mio Hirano1, Tatuya Yamamoto1, Naoki Takaya2,Motoyuki Shimizu1, Masashi Kato1

(1 Faculty of Agriculture, Univ. of Meijo 2 Univ. of Tukuba)

2 62 —

P-47 Aspergillus oryzae AdmA, AdmB

AdmA, AdmB , Aspergillus oryzae ADAM (A Disintegrin And Metalloproteinase) ADAM , g

, ∆admB ∆admA∆admB , RNA-Seq RNA-Seq

, , ´ , ADAM ADAM ,

g , AdmA AdmB C EGFP AdmA-EGFP, AdmB-EGFP glaA142

, A. oryzae niaD300 , , glaA142 AdmB-EGFP ,

, , SDS-PAGE , GFP , AdmB-EGFP GFP

AdmB-EGFP AdmB-EGFP , EGFP , AdmB-EGFP

g ,

Analysis on localization of AdmA and AdmB in Aspergillus oryzae

Takuji Kobayashi, Hiroshi Maeda, Michio Takeuchi, Youhei Yamagata

(Dept. of Applied Life Science, Tokyo Univ. of Agriculture and Technology)

P-48

1 1 2 3 1,2 1 2 3

― −g

´HPt RR MAP ´

HPt Aspergillus nidulans HPt (AnYpdA)

HPt (MgYpd1) MgYpd1 KT HPt RR

g KT KT HPt RR

HPt RR KT g g Mgypd1

AnypdA 9 YPD1 HPt 9 HPt ― KT

KT HPt

Analysis of the novel inhibitor “KT” of fungal tow-component signaling system by using yeast cells expressing

fungal HPt.

Fuka Tabata1, Mayumi Nakayama2, Akira Yoshimi2, Tomonori Fujioka3, Keietsu Abe1,2

(1Grad. Sch. Agric. Sci., 2NICHe, Tohoku Univ., 3Kumiai Chemical Industry Co., Ltd.)

2 63 —

P-49 (O-1)

terretonin Trt14

g g

Aspergillus terreus terretonin aterretonin Trt14 a

g L- [methyl-13C] methionineTrt14 g ´

1 Trt14 Trt14 His6

X Trt14˚ a Trt14

g A. oryzae NSAR1 terertonin andrastin A austinol

Trt14 gTrt14

a 1 Matsuda, Y., Iwabuchi, T., Wakimoto, T., Awakawa, T., Abe, I. J. Am. Chem. Soc., 137, 3393-3401 (2015)

Structural and functional studies on Trt14, a unique isomerase involving in the biosynthesis of terretonin

Taiki Iwabuchi, Yudai Matsuda, Takahiro Mori, Ikuro Abe

(Graduate School of Pharmaceutical Sciences, Univ. of Tokyo) P-50 Aspergillus oryzae

A. oryzae RIB40APase 11

g 11 APase 3pepO 5a a APase

mRNAPepO pepO

a pepO a

RIB 40 30 40 % g antipain g

antipain AorsinA Z-Arg-Arg-MCAAMC pepO AorsinA

g pepO aorA aRIB40 pepO aorA

CPase AorsinB aa

Analysis of extracellular proteases in Aspergillus oryzae acidic proteases deletion strains

Ayako Ueno, Hiroshi Maeda, Yohei Yamagata, Michio Takeuchi

(Division of Applied Biological Chemistry, Tokyo Univ. of Agriculture and Technology)

2 64 —

P-51 Emericella variecolor

β 5 a g 5

a 9 9 gg 9 9 g

a 9

9 g g 9Emericella variecolor 9

9 stellatic acid −gg P450 2 9stellatic acid

Emericella variecolor 9 9

a g , 9 9 9 g ,

9 a

The search for sesterterpene synthases from Emericella variecolor

Takaaki Mitsuhashi, Yudai Matsuda, Takahiro Mori, Takayoshi Awakawa, Ikuro Abe

(Graduate School of Pharmaceutical, Univ. of Tokyo)

P-52

Aspergillus oryzae β

A. oryzae 9 −g A. niger PhyA

8 Aph aphA aphH9 A. oryzae KBN630 aphA aphH 9aphAaphC 9AphA AphC9 9 aph

9A. oryzae aphB, aphD, aphE, aphF, aphG, aphH 9A. oryzae

a taaG2A. oryzae PDE1 alp pyrG 9

100 Aph 9 SDS-PAGE 9aphGAphG

AphG 99 g 9aphB, D, E, F, H

9Aph g

Studies on Acid Phosphatase Genes from Koji Mold, Aspergillus oryzae

Shoko YOSHINO-YASUDA, Natsuko ONO, Osamu HASEGAWA, Hironobu Mano (Food Res. Center, Aichi-Inst)

2 65 —

P-53 (O-2) Tricholoma matsutake

1 1 2 1 1

1 , 2

(Tricholoma matsutake)

g- - 9

a gg

g − 99 PCR

T.matsutake NBRC30605 1 % Yeast Extract 0.5 % 30mRNA cDNA PCR

g

” ga

Expression analysis of polysaccharide hydrolyzing enzyme genes from Tricholoma matsutake.

Hiroki Onuma1, Yasuhisa Fukuta1, Mizuho Kusuda2, Takao Terashita1, Norifumi Shirasaka1

(1Grad-Sch. Agri., Kindai Univ., 2Grad-Sch. Life Env. Sci. Osaka Prefec Univ.)

P-54 Lentinula edodes

S-PI Streptomyces-Pepsin Inhibitor

” Talopeptin

” a 9 9 ´

g

1 FeorestGEN

16 Eqolisin 4 Pepsin

7 Metallo protease 5

AUGUSTUS01_g7597.t1 g10028,t1 g867.t1 g2267.t1

JSPS 26870730

Expression analysis of protease genes from Lentinula edodes

Yasuhisa Fukuta, Takao Terashita, Norifumi Shirasaka

(Grad-Sch. Agri., Kindai Univ.)

2 66 —

P-55 Trichoderma reesei BGLII 1 1 2 1 2 1 1 2

Trichoderma reesei

T. reesei β- BGL

PC-3-7 T. reesei−g PC-3-7 BGL

BGLII gBGLII PC-3-7

T. reesei BGLII PC-3-7BGLII gg

Escherichia coli PC-3-7 BGLII 20BGLII HPLC TLC

BGLIIA L I S T C BGLII

a

The physiological role of BGLII in Trichoderma reesei

Ayana Nakamura 1, Machiko Takahashi 1, Yosuke Shida 1, Tomohiko Matsuzawa 2, Katsuro Yaoi 2, Wataru Ogasawara 1

(1 Nagaoka Univ. of Tech., 2 AIST)

P-56

Aspergillus nidulans GH 134 family β-1,4- Man134A

1, 1, 1, 1, 1, 1, α 1, 1, 1, 1, 2, 1 (1 , 2 )

9β- Aspergillus nidulans

9 β-1,4- glycoside hydrolase family 5 (GH5) GH26 gβ-1,4- (Man134A) 9A. nidulans

Man134A 50% 3 9Man134Ag3 g

man134A (Δman134A ) 99β- 9 (WT ) Δman134A

g 9Man134A β- 9Man134A Man5C 9β-

9 g g 9Man5C pH 4.0 Man134A 6.0 pH4.0 6.5 Man134A Man5C

9pH6.5 9Man134A β-93 a

Functional analysis of a novel β-1,4-mannanase Man134A and its homologs belonging to the new GH134 family

Kiyota SAKAI 1 , Mai MOCHIZUKI 1 , Miyuki YAMADA 1 , Yuhei KANEKO 1 , Saaya ISHIHARA 1 , Shinzawa

Yuta 1 , Minezawa Miho 1 , Kimoto Saran 1 , Sadanari JINDOU 2 , Tetsuo KOBAYASHI 3, Motoyuki SHIMIZU 1,

Masashi KATO 1 (1,2 Meijo Univ. , 3 Nagoya Univ.)

2 67 —

P-57 g NRPS-PKS

CSRS

1957 Alternaria tenius9 Magnaporthe oryzae g

9M. oryzae

M. oryzae 1 p38 MAP´ OSM1DMSO” a

MGG_07803MGG_07803 g

MGG_07803 (TAS1; Tenuazonic acid synthetase 1) gTAS1 NRPS-PKS PKS KS

S. cerevisiae TAS1 TAS1 isoleucine acetoacetyl-CoAKS KS

type I PKS KS 9type I PKS KS g

SIP

Biosynthesis of the mycotoxin tenuazonic acid by a novel fungal NRPS-PKS hybrid enzyme

Choong-Soo Yun, Takayuki Motoyama, Hiroyuki Osada

(Chem. Biol., RIKEN CSRS)

P-58

Phanerochaete chrysosporium PQQ

1 2 1 2 1 1 1 2

Coprinopsis cinerea PQQ CcSDHPQQ

PQQCcSDH

CcSDH g Phanerochaete chrysosporium PQQ

0.4 mM 4 mM 40 mM 6P. chrysosporium 3 cDNA cDNA

RT-PCR40 mM

g

Expression analysis of a novel pyrroloquinoline quinone-dependent oxidoreductase gene from the basidiomycete

Phanerochaete chrysosporium

Kohei Toya1, Kiwamu Umezawa2, Takuya Ishida1, Makoto Yoshida2, Kiyohiko Igarashi1, Masahiro Samejima1

(1Univ. Tokyo, 2Tokyo Univ. of Agric. and Technol.)

2 68 —

P-59 Aspergillus nidulans β-D-

β Aspergillus g (Galf)

Galf β-D- (Galf-ase) 9Galf−g A. nidulans Galf-ase Galf

α-L- (Araf-ase) Galf-ase9A. nidulans Araf-ase Galf-ase Galf-ase

Galf-ase Galf gGalf-ase A. nidulans Galf-ase

2 a 2 a Galf gGalf-ase A. nidulans 2a (AN2395, AN3200)cDNA pNP-Galf

pNP-Araf pNP AN2395, AN3200AN2395 His-Tag Araf-ase Galf-ase

AN3200 Araf-ase Galf-aseAN3200 A. nidulans Galf g Galf-ase g

Characterization of β-D-Galactofuranosidases in Aspergillus nidulans

Saki Toyota, Nao Yairo, Emiko Matsunaga, Yujiro Higuchi, Masatoshi Goto , Kaoru Takegawa

(Dept. of Biosci. & Biotechnol., Fac. of Agric., Kyushu Univ.) P-60

D- D-LDH , , ( )

a (PLA) 9 9

9 g 9PLA g

9 Aspergillus oryzae (LDH)9 g (1) 9

9 Nostoc D-LDH 51%

A. oryzae 9 BL21(DE3) pET9Ni 9

SDS-PAGE 41 kDa 9Nativeg 9 a

(1) 92007 − 9p179

Overexpression of D-lactate dehydrogenase (D-LDH) gene found from Aspergillus oryzae genome in Escherichia

coli and its enzymatic characterization

Akira Watanabe, Yoko Satoh, Katsuya Gomi

(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ.)

2 69 —

P-61 Aspergillus fumigatus

β

9 g

9 −9 g 9

g −g9 g

9 g 9 99 g 9 Aspergillus fumigatus 9

9 g RNA-Seq 99 592

9247 9 g g 99 9

9 g9 a 9

Transcriptome analysis in the responses to multi environmental changes in Aspergillus fumigatus

Hiroki Takahashi, Yoko Kusuya, Azusa Takahashi-Nakaguchi, Mariko Hayakawa, Tohru Gonoi

(MMRC, Chiba Univ) P-62

1

AtfA β

Aspergillus UV g− g

gAspergillus A. fumigatus, A. niger, A. oryzae RNA-seq

1hAf: 687 ; An: 694 ; Ao: 812 Af: 766 ; An: 1241 ; Ao:

749 g AspergillusBLAST 6172

a 91 391 gAtfA

A. fumigatus atfAAtfA g

atfA sterol rich domaing g g Aspergillus

/ AtfA a

Comparative transcriptome analysis in resting conidia and germinated conidia of three Aspergillus species

Daisuke Hagiwara, Yoko Kusuya, Hiroki Takahashi, Susumu Kawamoto, Katsuhiko Kamei, Tohru Gonoi

(MMRC, Chiba Univ.)

2 70 —

P-63 (O-7) Cag1

cap-growthless1g 9

cag1 cag1 Tup1 ga Tup1 9Cc.tupA

Tup1 9 DNA 9DNA9 Cag1

9 326 9Total RNA cDNA Cag19Yeast two hybrid 9 484000 cDNA

9 a Cag1 Interacting Protein CIP29CIP39CIP13a 9 CC1G_152879CC1G_116989CC1G_12764

PSORTII 99 Cag1

A screen to identify proteins interacting with Cag1 involved in cap growth of Coprinopsis cinerea.

Ryo Masuda, Hajime Muraguchi

(Dept. of Biotechnology, Akita Prefectural Univ.)

P-64

´ , ,

Aspergillus oryzae ´ ocpG ocpG 3 a g

1 2 g 1)

ocpG ˚ ocpG ocpG

ocpG ocpG ´ g

pepO pepO pepO 1 ocpG 1 ocpG 2 a

Czapek-Dox 24 pepO ocpG ocpG 1 ocpG 2 pepO

g ocpG ocpG 1 pepO 1 a Czapek-Dox 24

ocpG pepO 1 pepO 1 ocpG g g ocpG

´ g 1) Ishida K, et al., Biosci. Biotechnol. Biochem., 2014;78:1328-1336.

The sequence dependence of the intron retention in mRNA from A. oryzae serine-type carboxypeptidase gene

Ken Ishida, Michio Takeuchi, Youhei Yamagata (Dept. of Applied Biological Science, Tokyo Univ. of Agriculture and

Technology)

2 71 —

P-65

β ℃

, g, (CCR) ,

, CCR 9 A. oryzae , CCR , , CreACCR , Czapek-Dox

, ” , A. oryzaeg g , ,

CCR g 2% , ˚ ˚

, 100 mM ” ” , A. oryzae Δku70( ) ΔcreA, Δku70 , 9˚ , CCR , ˚

, CCR ΔcreA, Δku70 , ˚, CCR , CreA g

CCR , g Carbon catabolite repression for amylase production in Aspergillus oryzae is affected by the deference of nitrogen sources

Masahiro Ogawa, Yasuji Koyama

(Noda Institute for Scientific Research)

P-66 Aspergillus terreus pH

´

” A. terreus

´ CADCAD1 CAD

pH2 3pH4 •

pH pH2 3 g pH5

CAD1 CAD pH2 3 pH5 CAD1CAD pH g

CAD1 Regulation of pH responsive itaconic acid production in Aspergillus terreus Yoshiki Ando1, Katsuya Obana1, Shin Kanamasa2

(1Grad. Sch. Biosci. Biotech. Chubu Univ., 2Dept. Envi. Biol. Chubu Univ.)

2 72 —

P-67 HypD

g 8a Cys Aspergillus oryzae 4a (HypA-D)

HypD 207 C 63 93 g C g

g a HypD a

in vitro HypD HypDHypD HypD

/

in vivo HypD - (GUS) hypDhypD

g g ―hypD ―

HypD

Characterization of a hydrophobin HypD from Aspergillus oryzae

Kandai Ishikura, Yuki Fujii, Takahiro Tsuchiya, Takuya Inaba, Harushi Nakajima

(Dept. of Agricultural chemistry, Univ. of Meiji)

P-68

CreA

C2H2 CreA ,

CreA , g, 14

, CreA CreA a

, GFP CreA N GFP CreA creA

, ,

, ´ , , CreA nuclear export signal (NES)

, NES CreA , ´, NES CreA

, CreA g, CreA ,

Involvement of subcellular localization in the stability of glucose repression regulator CreA in A. oryzae.

Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi

(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ.)

2 73 —

P-69 Srs2 DNA

β 1 ” 2 3 3 1 1 1 1 2

3

DNA DSBs HR− Srs2

DNA Srs2 DNAsrs2

Scytalone dehydratase SDHsrs2 HR

srs2 100srs2 • g HR

The role of Srs2 DNA helicase in homologous recombination repair mechanism of Pyricularia oryzae

Tetsuo Ogawa1, Takayuki Arazoe2, Tetsushi Sakuma3, Takashi Yamamoto3, Shigeru Kuwata1, Kohji Kusano1, Shuichi

Ohsato1

(1Grad. Sch, Agric., Meiji Univ., 2Grad. Sch, Eng., Kobe Univ., 3Grad. Sch, Sci., Hiroshima Univ.)

P-70 Transcriptional regulation mechanism of Trichodermapepsin in Trichoderma reesei Nayani D. Daranagama, Hiroki Aita, Hiroki Hirasawa, Koki Shioya, Haruna Sato, Yoshiyuki Suzuki, Yosuke Shida,

Wataru Ogasawara (Dept. of Bioeng., Nagaoka Univ. of Tech.) Fungal proteases play critical role in metabolism, nutrition and morphogenesis. Filamentous fungus Trichoderma reesei which is a most potent cellulase producer and used in many industrial applications, produces the aspartic protease called Trichodermapepsin (TrAsP). TrAsP is involved in proteolytic degradation of cellulases in culture medium. Generally, Production of extracellular proteases is regulated at transcription level and protein level. Previously, we presented that TrAsp was induced by monosaccharides, especially galactose and not expressed in cellulase inducers such as cellulose and sophorose. This disclosed that carbon based regulating mechanism existed in TrAsP production. However, regulation system of proteases T. reesei was not studied in detail and a relationship between cellulase and protease production mechanism is still unknown. Due to paucity of knowledge of TrAsP, objective of this study is ascertaining TrAsP producing mechanism. The promoter region of TrAsP of T. reesei QM9414 has putative binding sequence of XYRI, ACEI, CREI, AREA and PACC, that are regulating cellulase production. Specially, XYRI is an essential transcription factor and AREA regulates nitrogen metabolism. Interestingly, results of promoter deletion GUS reporter analysis suggest that XYRI and AREA act as a repressor and an activator in respectively for TrAsP production. For further confirmation, deletion strains of these transcription factors in QM9414 were cultivated in cellulose, glucose and galctose and measured protease activity of culture supernatants separately. Both in glucose and galacotose medium, protease activity of QM∆xyr1 significantly increased, but QM∆areA didn’t show protease activity. It reveals that TrAsp production is not only depended on carbon source, but also nitrogen source in the medium and cellulase regulating transcription factors differently involve in protease production. This insight of regulation mechanism of TrAsP shows a novel avenue for celluase production mechanism in filamentous fungi.

2 74 —

P-71 (O-6) Binding features of ManR and ManS involved in cellulase and mannanase regulation in Aspergillus nidulans Nuo Li Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi (Grad. Sch. Bioagric. Sci., Nagoya Univ.)

In A. nidulans, ManR regulates the expression of cellulolytic genes together with McmA by being recruited to CeRE

(Cellulose Responsive Element). Regulation of mannanase production is under control of both ManR and its paralog ManS. Cellobiose induces some mannanase genes (manB, manC, mndB) in a ManR dependent manner, while galactomannan induces a different set of mannanase genes (manC, manE, manF), for which ManS is responsible. In this report, we identified the sequence in CeRE recognized by ManR and showed the relationship between ManR and ManS in binding to some manannase genes.

Mutation analysis by EMSA on CGG/CCG that is within and close to CeRE on the promoter of endoglucanase gene, eglA and eglB, showed that CCG triplet in CeRE serves as ClrB recognition sequence. ManS could bind to the same 3 sites (CGGN8CCG) as ManR does on the promoter of mndB. However the 2nd binding site which showed the weakest binding affinity by ManR turned out to be bound most strongly by ManS among the three binding sites. In additionpromoter activity assay showed reporter gene with the 2nd binding site was induced in galactomannan, concerning that it is inactive in CMC. These findings indicates that ManR and ManS may possess opposite effect in regulating mndB under different inducers. In the case of binding to manB, manE and manF, both ManR and ManS can recognize CGGN9CC/GG, while most interestingly is when they were added together to the reaction, ManR-ManS heterodimer was formed. This result aroused our interest in investigating the roles of ManR and ManS in regulation of mannanase genes. Further study will focus on the clarification of inductive mechanism mediated by ManR and ManS, and the necessity of heterodimer formation.

This work was supported by the Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry and the Science and technology research promotion program for agriculture, forestry, fisheries and food industry. P-72

Aspergillus oryzae PhoR , , ,

Saccharomyces cerevisiae Pho4p 9 9

g 9 aAspergillus nidulans PalcA Aspergillus oryzae PhoR 9

9 9 RIB40 ΔligDΔpyrG phoR 9 phoR

9 (0.1mM) 9 g9 • (11mM)

9 g g 9 •9 11 a qRT-PCR

96 phoR •g 2 • 9phoR

9 24 g 940• 9GFP-PhoR 9

Functional analysis of the transcription factor involeved in phosphate acquisition in Aspergillus oryzae

Sawaki Tada, Hikaru Ohkuchi, Satoshi Suzuki, Ken-Ichi Kusumoto (NFRI NARO)

2 75 —

P-73 (O-5) g

Aspergillus oryzae ESTenoA 3 gpdA 2 a

2 a genoA 2a

g 5,UTR2

a g−g 5,RACE qRT-PCR enoA gpdA

− 3 15,UTR gg fbaA enoA g

− AcuK9AcuM enoA2015 fbaA

ORF AcuK AcuMAcuK AcuM a

Identification of glycolytic genes transcribed alternatively depending on carbon sources in Aspergillus oryzae

Taishi Inoue, Hiroki Toji, Mitsuru Takama, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi

(Div. Biosci. Biotechnol. Future Bioind., Grad. Sci. Agric. Sci, Univ. of Tohoku)

P-74

XlnR 9 β 9 9 9

XlnR ´ ´

9 ´ 99´ 9 XlnR

9 g 9XlnR 69

´ 9S556AXlnR ´ xynG2

Northern blotting 9 mRNA 9XlnRWestern blotting S556A 9 ´

g 2 isoform 9 isoform9S556 XlnR 9xynG2

g 99´ g a9 9

Physiological role of inducer-triggered phosphorylation of XlnR in Aspergillus oryzae.

Koji Asai, Kengo Sugimoto, Shuhei Ishikawa, Kyoko Kanamaru, Makoto Kimura, and Tetsuo Kobayashi

(Grad. Sch. Bioagric. Sci, Nagoya Univ.)

2 76 —

P-75 α- MalT

β β-

AmyR AmyR ag g −g

MalP α- MalTMalR g (MAL cluster)

−g MalT amalT 9

α - g α - g

malTmalT g

AmyR MalTMalT 9

Involvement of an intracellular α-glucosidase, MalT, in inducible production of amylolytic enzymes in

Aspergillus oryzae

Takayasu Watanabe, Takanori Ichikawa, Sachiko Hasegawa-Shiro, Mizuki Tanaka, Akira Watanabe, Takahiro Shintani,

Katsuya Gomi (Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ. )

P-76 Aspergillus oryzae csrA natural antisense RNA sense RNA

EST csrA (conidia specific

reductase) g antisense RNA (as-csrA) EST 528 EST 43 PCR as-csrA

csrA sense RNA (SN RNA)

csrA (∆csrA ) (1) CsrA as-csrA

total RNA S1 nuclease RT-PCR mRNA csrA mRNA

as-csrA (∆as-csrA) ∆csrA ∆csrA ∆as-csrA

∆as-csrA g CsrA as-csrA as-csrA SN RNA csrA mRNA

(1) M Tsujii et al, Biosci Biotech Biochem, in press. doi: 10.1080/09168451.2015.1101333.

Natural antisense RNA of csrA binds to sense RNA and regulate germination in Aspergillus oryzae

Masaru Tsujii Michio Takeuchi Youhei Yamagata

(Department of Applied Biological Science Tokyo University of Agriculture and Technology)

2 77 —

P-77 Fusarium graminearum Tri6 5'

Fusarium graminearum ´

9 Tri6 P450 ´ Tri49 1.1 kb

GATA g g 9Tri4 370 bp TRI6Tri4 9 Tri6

gTri6 9 Tri4-Tri6

a 9 Tri4 TRI6

9 9Tri4 9 9

Tri4 TRI6 Tri4g Tri6 9

Functional analysis of Tri6 5' upstream region in Fusarium graminearum.

Yuichi Nakajima, Kazuyuki Maeda, Kyoko Kanamaru, Tetsuo Kobayashi, Makoto Kimura

(Graduate School of Bioagricultural Sciences, Nagoya Univ. )

P-78 抗摂食性物質 citreohybridonol合成を担うシトクロム P450の発見 全智揚，松田侑大，阿部郁朗 （東大院・薬）

メロテルペノイドとはテルペノイドの部分構造を有する化合物の総称である。我々は，糸状菌メロテルペ

ノイドの生合成に興味を持ち，andrastin A，terretonin，anditomin を始めとするメロテルペノイド化合物の生合成研究を展開してきた。我々は新たに andrastin A の生合成遺伝子クラスター（adr クラスター）と類似した遺伝子クラスターを Emericella variecolorのゲノム中に見出しており，本クラスター特異的に含まれる 3つの遺伝子を andrastin A生産能を有する Aspergillus oryzae形質転換体に導入することで，新規代謝物が得られることを報告している 1。 今回，この新たに得られた化合物の単離構造決定を試みたところ，本化合物が抗摂食作用を有する

citreohybridonol であることが判明した。加えて，citreohybridonol の生合成中間体と考えられる新規化合物の単離構造決定にも成功した。一方で，上述の 3 つの遺伝子のより詳細な機能解析を行ったところ，citreohybridonolの生合成に寄与するのはシトクロム P450をコードする 1つの遺伝子のみであることも明らかとなった。現在，citreohybridonolに至る生合成経路の確立ならびに、本 P450に由来する未知の生合成前駆体の構造決定を進めており，その結果についても合わせて報告したい。

1. 全ら，第 14回糸状菌分子生物学コンファレンス要旨集，2014，P-84

Discovery of a cytochrome P450 responsible for the synthesis of an antifeeding compound citreohybridonol

Zhiyang Quan, Yudai Matsuda, Ikuro Abe

(Graduate School of Pharmaceutical Sciences, Univ. of Tokyo)

2 78 —

P-79 An unusual chimeric terpene synthase from Emericella variecolor: Diterpene synthase or sesterterpene synthase? Bin Qin Takahiro Mori Yudai Matsuda Masahiro Okada Takaaki Mitsuhashi Zhiyang Quan Ikuro Abe The

University of Tokyo Graduate School of Pharmaceutical Sciences Diterpene synthases are the primary enzymes responsible for catalyzing the formation of diterpenes (C20) from the

substrates GGPP (Geranylgeranyl pyrophosphate), while sesterterpene synthases are responsible for the forming of sesterterpenes (C25) from GFPP (Geranylfarnesyl pyrophosphate). In this research, by genome mining of E. variecolor, we found a chimeric terpene synthase consisting of cyclase domain and prenyltransferase domain. The metabolite of this chimeric terpene synthase was identified as a diterpene compound by using in vivo system (Aspergillus oryzae). Surprisingly, besides the diterpene compound, this terpene synthase could produce a sesterterpene compound in vitro by using DMAPP (Dimethylallyl pyrophosphate) and IPP (Isopentenyl pyrophosphate) as substrates. To investigate the structure of the sesterterpene compound, a new chimeric terpene synthase was constructed by swapping the PT domain of this terpene synthase with a GFPP synthase from E. variecolor, and as a result, the chimeric enzyme could produce both diterpene and sesterterpene compounds in vivo. These findings indicate that this terpene synthase is an unusual terpene synthase, which displays the ability to catalyze the forming of both diterpene and sesterterpene compounds. The absolute configurations of the two metabolites were also determined in this research.

An unusual chimeric terpene synthase: Production of diterpene and sesterterpene at the same time

Bin Qin Takahiro Mori Yudai Matsuda Masahiro Okada Takaaki Mitsuhashi Zhiyang Quan Ikuro Abe

Grad. Sch. Pharm. Sci. Univ. of Tokyo P-80 (O-3)

Lecanicillium sp. PKSNRPS

, Minh Viet Nguyen, , ,

PKS NRPS −g

Lecanicillium sp. MAFF635047 PKS NRPS ,

9 , PKS NRPS a

PKS NRPS

g ,

Lecanicillium sp. MAFF635047 PKS , NRPS 9

a HPLC ,

g , MS , NMR

9fusaristatin g

Identification of a novel hybrid compound synthesized by PKS and NRPS from Lecanicillium sp. MAFF635047

Miyuki Nakamura, Minh Viet Nguyen, Keiichi Ishido, Hiroshi Kinoshita, Takuya Nihira (ICBiotech, Osaka Univ.)

2 79 —

P-81 cpaM

1, 2, 2, 3, 4,5, 4, 3, 2, 2, 2 (1 , 2 , 3 , 4 , 5

(CPA) Aspergillus oryzae

, A. oryzae CPA cpaA, cpaD, cpaO , CPAcpaH cpaM 1) cpaH , CPA2-oxoCPA , cpaM , g , gg 1) CpaM , A. oryzae 2-oxoCPA

speradine A g , cpaM speradine A , A. oryzae g , cpaM

speradine A A. tamarii NBRC 4099 a , cpaM ORFcpaM A. oryzae , 2-oxoCPA speradine

A , A. tamarii cpaM ORF 4˚ , 4˚cpaM A. oryzae , speradine A , cpaM speradine A

g , , A. oryzae cpaM 4˚ g

1) Kato, N. et al., ChemBioChem 12, 1376–1382 (2011)

Functional analysis of the cpaM in cyclopiazonic acid biosynthesis

Tomoki Kikuchi1, Akifumi Koyama2, Shin-ichiro Iio2, Yasutomo Shinohara3, Takaaki Kubota4,5, Jun-ichi Kobayashi4,

Yasuji Koyama3, Masafumi Tokuoka2, Hitoshi Shindo2, Masaru Hosaka2 (1Grad. Sch. Agric., Tokyo Univ. Agric., 2Fac.

Appl. Biosci., Tokyo Univ. Agric., 3Noda Inst. Sci. Res., 4Grad. Sch. Pharm., Hokkaido Univ., 5Showa Pharm. Univ.)

P-82 Aspergillus kawachii 1 2 1 1 1 3 1 1 1

2 3

Aspergillus kawachii acitA

9 RNAnrd1 ´ yhm2

nrdA yhmA citA yhmA citA yhmA

g9citA •

yhmA 9 ´• yhmA citA nrdA

Characterization of genes associated with citrate synthesis in Aspergillus kawachii

Chihiro Kadooka1, Kosuke Izumitsu2, Kayu Okutsu1, Yumiko Yoshizaki1, Kazunori Takamine1, Masatoshi Goto3,

Hisanori Tamaki1, Taiki Futagami1

(1Kagoshima Univ., 2Univ. of Shiga Pref., 3Kyushu Univ.)

2 80 —

P-83 (O-4) astellolide

1 β 2 2 2 1 1 92 CSRS

9 g 9g g 9

g 9 99 9

9 3 4cclA ΔcclA 9 a

9 2 a 914-deacetyl astellolide A (14-DAA) B (14-DAB)

914-DABg 9astellolide

9ΔcclA 9NRPS astA ΔcclA 9

ΔcclA 9 (ΔcclA ΔastA) LC-MS9ΔcclA ΔastA 914-DAA 14-DAB 9astA astellolide

g

Identification of astellolide biosynthetic gene cluster in Aspergillus oryzae.

Yasutomo Shinohara1, Makoto Kawatani2, Yushi Futamura2, Hiroyuki Osada2, Yasuji Koyama1

(1 Noda Ins. Sci. Res., 2RIKEN CSRS)

P-84

1 2 1 1 2 1 1 CSRS2

Penicillium simplicissimum AK-40

gg

a g P. simplicissimum AK-40

2ndFindNRPS ´

NRPSa oka 9

oka a oka9 LC/MS 4

´oka g

Identification of the okaramine biosynthetic gene cluster

Naoki Kato1, Shogo Furutani2, Kiyomi Kinugasa, Shunji Takahashi1, Kazuhiko Matsuda2, Hiroyuki Osada1

(1Chem. Biol., RIKEN CSRS, 2Dept. of Agri., Kinki Univ.)

2 81 —

P-85 Sirtuin

Aspergillus nidulans NAD+ sirtuin (SirA)g

sirA 4 a sirtuin sirB sirC sirD sirEH4K16g 5 a sirtuin

1107 SirA 317 SirA A. nidulans

SirAdiorcinol cordyol C violaceol I violaceol II 0.5 mM diorcinol ”A. nidulans A. terreus Ustilago maydis Fusarium oxysporum diorcinol ” g

gdiorcinol

g

Sirtuins regulate fungal secondary metabolisms

Ryosuke Shigemoto, Eriko Ito, Shuhei Harimoto, Takara Matsumoto, Shunnsuke Masuo and Naoki Takaya

(Faculty of Life and Environmental Sciences, Univ. of Tsukuba)

P-86 (O-8)

β 9

542012 9

RNA-Seq9

g

Mathematical Modeling for Mycorrhizal Infection using Biological Big Data and Combinatorial Optmization

Kazuo Ishii , Toshinori Kozaki , Tomomi Nakagawa

( Tokyo Univ. Agricul. Technol., Natl. Inst. Basic Biol.)

2 82 —

P-87 g -´

´−g Wegener et al. (1999)

Bipolaris zeicola −g -´ Xyp1 Xyp1 Glycoside Hydrolase 43 ´ g

B. maydis Xyp1BmXyp1 BmXyp2 2a

Xyp1 BmXyp1Bipolaris a BmXyp2 BmXyp1

Aspergillus oryzaeg BmXyp2g BmXyp1 g

B. maydis BmXYP1´2% (w/v) ”

gg

BmXyp2a

Expression assay of a putative beta-xylosidase homologue whose phyletic group is unique to Pleosporales fungi

Hiroshi Yoshida, Takuya Sumita, Chihiro Tanaka

(Grad. School of Agriculture, Kyoto Univ.)

P-88 ´ g β 1 2 3 4 3 3

1 2 CSRS 3 4

´ Fusarium oxysporum f. sp. conglutinans Foc FocSIX4 1.4 Mb

, 2014 f. sp. pisi f. sp. lycopersici FolColeman et al., 2009, Ma et al., 2010

Fol −g conditionally dispensable CD Ma et al., 2010 Foc

a BFoc Kashiwa et al., 2013 9VanEtten et al. 1998 1.56

70.0 µg / ml B 5, 1.4 Mb 2.2 Mb g 1 DNA

1.4 Mb SIX9 ORX1, 2.2 Mb SIX8PCR 2

25 °C 9 PDAg 1.4 Mb 2.2 Mb Foc g

Dispensable small chromosomes in Fusarium oxysporum f. sp. conglutinans

Yu Ayukawa1, Takeshi Kashiwa2, Ken Komatsu3 4, Tohru Teraoka3, Tsutomu Arie3

(1 Unit. Grad. Sch. Agric., Tokyo Univ. of Agric. Tech. 2 CSRS, RIKEN 3 Grad. Sch. Agric., Tokyo Univ. of Agric.

Tech. 4 Organization for Promotion of Tenure-track System, Tokyo Univ. of Agric. Tech.)

2 83 —

P-89 (O-9) AVR-Pia

1 1 1 2 3 1 1

1 , 2 3

−AVR R

g AVR 1 a AVR-Pia R PiaPia 1 a RGA5-A C

Yeast two hybrid AVR-Pia 2 AVR-PiaF38AV40A AVR-Pia AVR-PiaF38AV40A

Pia 1a RGA5-A CAVR-PiaF38AV40A Pia

Δ AVR-PiaNMR AVR-Pia 6a g

g AVR AVR-Pizt Pyrenophora tricici-repentis ToxB

Structure and Function of AVR-Pia Protein of Magnaporthe oryzae

Shiho Fujiwara1, Yuya Highchi1,Yuki Satoh1, Toyoyuki Ose2, Masakatsu Kamiya3, Kozo Asano1, Teruo Sone1

(1Grad. Sch. Agriculture, 2Fac. Pharmaceutical Sci., 3Fac. Adv. Life Sci., Hokkaido Univ.)

P-90 Aspergillus fumigatus

β

9 g 9 g 9

5 − 9 g

g 9 9

Cryptococcus neoformans 9 Cuf1

9 − Aspergillus

fumigatus 9

9A. fumigatus 9

g A. fumigatus 9RNA-seq 9A. fumigatus

9

170 9 ´ 104

9A. fumigatus 9

5 C. neoformans 3a 9

The molecular mechanisms of copper acquisition and detoxification in Aspergillus fumigatus

Yoko Kusuya, Mariko Hayakawa, Tohru Gonoi, Hiroki Takahashi

(MMRC, Chiba Univ)

2 84 —

P-91

1 2 1 1 1 1 2

Fusarium oxysporum f. sp. lycopersici 3a3 a a AVR a

1 3a AVR1 AVR2 AVR3 AVRI9 I29 I3 g

AVR1 I g avr1 1I i2 i3 g 2 g avr1 AVR2 AVR3

AVR1 AVR1 avr1null Houterman et al.,2008ORF avrth380

Inami et al.,2012 avrth658 2013 ORF AVR1g avr1tf-380 2015 3 AVR2

ORF G121A T122A G134A G137C C146T 5Houterman et al., 2009 2012 2014 18-1

PCR AVR2 g avr2null 18-1g

g

The diversity of mutations of avirulence genes of the tomato wilt fungus Fusarium oxysporum f. sp. lycopersici

Kotaro Akai1, Sakiko Tamura2, Ken Komatsu1, Toru Teraoka1, Tsutomu Arie1

(1Grad. Sch. Agric., Tokyo Univ. of Agric. Tech., 2 Fac. Agric. Tokyo Univ. of Agric. Tech.)

P-92 ´ ´

´ (Corynespora cassiicola) g ´g ´

a

´ ―´ OS-1 ´ (― )

(9-12 ) (20-1 ) CcOS1 PCRCcOS1 ´ 25bp (

) 132 g25bp

4 g No.20a g beta-tubulin F200Y

( ) “

Identification dicarboximide- and phenylpyrrole-resistant mutation in Ccos1 gene of Corynespora cassiicola

Yoshihito Tsukada, Reina Horiuchi, Akihiko Ichiishi, Makoto Fujimura

(Life Sciences, Toyo Univ.)

2 85 —

P-93 Hope

Vy Trinh Thi Phuong

Pyricularia oryzae g

a gBr58 Rwt3

Rwt4 PWT3 PWT4Rwt3 Rwt4 g Hope Br58

Br58 x 76Q1 Br48 x Br58 F1Hope 1:1

g 1PWTX 80

PWTX 1.3cM248 9

fine mapping PWTX 0.4cM 2aBr58 BAC library

2a BAC

Identification and molecular mapping of genes involved in the incompatibility of an Avena isolate of Pyricularia

oryzae with wheat cultivar ‘Hope’

Kaori Komatsu, Ryota Mori, Yoshihiro Inoue, Vy Trinh Thi Phuong, Izumi Chuma, Yukio Tosa

(Grad. Sch. Agric. Sci, Kobe Univ.)

P-94 Epichloae Epichloë/Neotyphodium

1 2 3 2 1 1 1 2

Epichloae Epichloë/Neotyphodium ,

. , . , Epichloae , g

Neotyphodium , . , Neotyphodium Epichloë , epichloae

g . , Epichloae , ,

, , g , . , g, g .

, g g , . , epichloae

, , .

Characterization of hybrid strais of Epichloae Epichloë/Neotyphodium spp. endophyte produced via para-sexual reproduction. Hitomi Isobe1, Akira Masunaka2, Koya Sugawara3, Takao Tsukiboshi2, Aiko Tanaka1, Daigo Takemoto1 (1 Grad. School Bioagr. Sci., Nagoya Univ., 2 NILGS, 3 NARO, TARC)

2 86 —

P-95 26S RPN10

1 2 1 1 2

g ´ −g

9 gg g´ RPN10

RPN10− RPN10 CoRPN10

CoRPN10

g

−

The 26S proteasome subunit RPN10 homolog in Colletotrichum orbiculare is required for pathogenicity to the

host plant.

Takuya Sumita1, Kosuke Izumitsu2, Chihiro Tanaka1

(1Grad. School of Agriculture, Kyoto Univ., 2Sch. Of Environmental Science, Univ. of Shiga Pref.)

P-96 Epichloë festucae

1 1 1 1 1 Barry Scott2 3 1

1 1 2 Inst. Fund. Sci., Massey Univ. 3

E. festucae . , E. festucaeg −g , NoxA, G

GpaA Sog , g

, . , g .

NsiA Nuclear protein for Symbiotic Infection, . nsiA , ProA, Ham8, Pro41g

g , NsiA , . , Yeast two hybrid , NsiA g

MAP´ Mak2 Ste12. E. festucae mak2 , ste12

g . , nsiA ste12 , NsiA , Mak2 Ste12 .

Functional analysis of signaling factors for symbiotic infection and hyphal cell fusion of Epichloë festucae Shota Kamiya1, Ayane Okamura1, Yoshino Ozaki1, Shinichi Kameoka1, Yuka Kayano1, Barry Scott2, Jun-ichi Maruyama3, Aiko Tanaka1 and

Daigo Takemoto1 (1Grad. School Bioagr. Sci., Nagoya Univ., 2Inst. Fund. Sci., Massay Univ., 3Dept. of Biotechnol., The Univ. of Tokyo)

2 87 —

P-97 Colletotrichum orbiculare species complex9 β 1 1 2 3 Pamela Gan 4 4 2 1 1

2 3 4

70 600 g

Colletotrichum aC. orbiculare species complex (Cosc) 4 g n=10

AT-rich g a CoscC. lindemuthianum C. malvarum C. tebeestii AT-rich

n=10 Coscg CoSC CoSC

C. malvarum C. tebeestiiCosc

Colletotrichum orbiculare species complex conserves similar karyotype and partly shares common host.

Mami Ogawa1 Kaoru Tanaka1 Hitomi Kaminakaya2 Jun Yamashita3 Pamela Gan 4 Ken Shirasu4 Masatoki Taga2

Yasuyuki Kubo1

(1 Grad. Sch. of Life & Env. Sci., Kyoto Pref. Univ. 2 Grad. Sch. of Nat. Sci. & Tech., Okayama Univ. 3 Inst. of Plant

Sci. & Res. 4RIKEN)

P-98 WHI2 CoWHI2

TOR 1, 2, 1 ( 1, 2)

, CoWHI2

, cowhi2, CoWhi2 a , cowhi2

6h , cowhi24h , cowhi2

,10Fold g ,TOR(Target Of Rapamycine) , cowhi2

TOR ,TOR cowhi2, cowhi2

, ,CoWHI2 TOR, TOR ,

cowhi2cowhi2 , cowhi2 ,

• 9 , CoWHI2 TOR

CoWHI2, the homolog of stress response regulator WHI2 of Saccharomyces cerevisiae, is involved in regulation of

hemibiotrophic infection in Colletotrichum orbiculare through TOR pathway.

Ken Harata1, Takumi Nishiuchi2, Yasuyuki Kubo1

(1Life and Environmental Sciences, Kyoto Prefectual Univ., 2Advanced Science Research Centre, Kanazawa Univ.)

2 88 —

P-99 Aspergillus fumigatus

A. fumigatus g

g −g

a g

g g A. fumigatus

a

A. fumigatus fucose a (AFL) a

AFL 6 a fucose • a

AFL AFL

fucose g

AFL A. fumigatus g

Functional analysis of fcose-specific lectin from Aspergillus fumigatus.

Kanae Sakai, Tohru Gonoi

(MMRC, Univ. of Chiba)

P-100 Aspergillus fumigatus

→ 1 2 3 2 1 2 3

Aspergillus fumigatus g g9 9 9 g9 9 g 9

A. fumigatus 2 4 2 RNA 95 2 RNA 9

9 ORF ORF 99 A. fumigatus KU ORF9 g

4 2 RNA ORFc 95 2 RNA ORFb9ORFcORF a

9PCR 9 9 g 9

a

Influence of mycovirus ORF expression in human pathogen Aspergillus fumigatus.

Erika Shishido1, Azusa Takahashi-Nakaguchi2, Hiromitsu Moriyama3, Tohru Gonoi2

(1Grad. School of Medical and Pharm. Sci., Chiba Univ., 2MMRC, Chiba Univ., 3Tokyo Univ. of Agric. & Tech.)

2 89 —

P-101 (O-10) CLA4

1 2 1 1 1 92

− a 2 PAK

´ STE20g CLA4 , Δcla4 g, Δcla4 a

Δcla4 , ´ , Δcla4 ,

g g , , , Δcla4 FM4-64 ,

1 Spitzenkörper , Δcla4 0~2 CLA4− g , Δcla4 g

, 20 1CLA4 ,

Relationship between the CLA4 homologue and hyphal growth in Bipolaris maydis

Yuki Kitade1, Kosuke Izumitsu2, Takuya Sumita1, Chihiro Tanaka1

(1Grad. Sch. of Agriculture, Kyoto Univ., 2Sch.of Environmental Science,Univ. of Shiga Pref.)

P-102

MOR

1 1 1 2 1 3 1 1 2

3

NDR (nuclear Dbf2-related)´CoCbk1 CoPag1 MOR (morphogenesis-related NDR kinase network)

copag1CoCbk1 in vitro in planta

MORin vitro in planta

in vitro in plantacopag1 N

a CoCbk1CoCbk1

MOR

Study on the involvement of plant-derived signals in appressorium development by comparative transcriptome

profiling of Colletotrichum orbiculare MOR mutants

Sayo Kodama1, Jyunya Ishizuka1, Ito Miyashita1, Takumi Nishiuchi2, Takaaki Ishii1, Hideto Miyoshi3 and Yasuyuki

Kubo1

(1Grad. Sch. of Life & Env. Sci., Kyoto Pref. Univ., 2ASRC., Kanazawa Univ., 3Grad. Sch. of Agric., Kyoto Univ.)

2 90 —

P-103

, , , , ( )

9

9

9 g

g g 9 9

RIB40 9

g 9 9 92,4,6,8g 9 913 a

9 9

9

g 9 g 9 9

g 9 2 a g 9 29 g 9

9 g g 9

g 9 g

Comparative analysis of genome sequence and aspirochlorine productivity of Asperugillus oryzae strains

Ryota Saito, Tami Ohota, Miyuki Umeo, Ken Oda, Kazuhiro Iwashita

(Natl. Inst. Brew., Fundam. Res. Div.)

P-104 Aspergillus aculeatus

β

A. aculeatusT-DNA M1 Q3 2

2 Avicel Xylose´ qRT-PCR

M1 Xylose ´ Ib (xynIb) Q3 Avicel I (cbhI)

g A. aculeatusFI-CMCase (cmc1) M1 cmc1 xynIb

XlnR Q3 cbhI ManR

A. aculeatus

Phenotypic analyses of cellulose utilization deficient mutants in Aspergillus aculeatus

Ryohei Katayama, Syota Yuki, Shuji Tani, Junichi Sumitani, Takashi Kawaguchi

(Grad. Sch. Life & Env. Sci., Osaka Pref. Univ.)

2 91 —

Aita, Hiroki ........... 73

H

Bergs, Anna .... 34, 50

I

Daranagama, Nayani

D. ..................... 73 Dietrich, Helge M. . 54

Gan, Pamela ......... 87 Gao, Hao ............... 39

Hirasawa, Hiroki .... 73

Ishitsuka, Yuji . 34, 50

Li, Chang .............. 39 Li, Nuo ........... 31, 74

Nguyen, Minh Viet 30, 78

Nienhaus, G. Ulrich34, 50

Okada, Masahiro .... 78

Phuong, Vy Trinh Thi

........................ 85

Qin, Bin ................ 78

Sato, Haruna .......... 73

Scott, Barry ........... 86 Shioya, Koki .......... 73 Suzuki, Yoshiyuki .. 73

Yao, Xin Sheng ...... 39

.............. 43 ........... 84

.............. 75 ..... 39, 40

........ 33, 83 .............. 43 . 29, 39, 63,

64, 77 . 41, 43, 44,

45, 55, 59, 62 β .................. 82 ” .. 38, 50, 73

38, 50, 82, 84 42, 51, 52, 59

.............. 41 β .............. 64

........ 34, 51 .............. 71

........... 79 ....... 67

.................. 51 ........ 32, 81 .............. 89 .............. 60

β .............. 75 ............. 72

.................. 70 .............. 67 .............. 89 ........ 30, 78

........... 66 . 33, 79, 86,

89 ..................... 61

.............. 85 ........ 17, 84

β .............. 76 ................. 40

........ 37, 45 .............. 56

.......... 81 ............ 72

........ 31, 75 .............. 85 .. 35, 52, 90 ........ 29, 63

.............. 63 ........ 41, 43 .............. 56 .............. 90

................. 67 .............. 46

.. 58, 60, 61 ................. 44

.......... 74 .. 38, 50, 73

................ 90 ........ 29, 65

.......... 43 ........ 66, 73

..... 58, 60, 61 ........ 47, 48 . 35, 36, 42,

52 .............. 86

β .. 38, 50, 73 β ........ 52, 71 β .............. 87

........ 39, 40 .............. 79 .. 47, 48, 49

.... 47, 48, 49

........... 86 .. 30, 67, 80 ........ 33, 83

........... 42 .................. 90

........... 64 .............. 71

.............. 53 ..................... 82

........... 41 ..... 58, 61

. 36, 42, 54, 58

.............. 90 .............. 80 .. 36, 61, 66 .............. 79

.................. 71 . 31, 38, 49,

74, 75, 77 .............. 66

.................. 46 .............. 87 .............. 86 ........ 33, 83 .............. 69 .............. 86 .............. 86

β .............. 59 β .............. 90 β ........ 42, 54 β ............ 30, 80 β .............. 60 β .................. 69

2 92 —

全智揚 ............ 77, 78

.............. 79 ........ 57, 59 ........ 33, 89

... 35, 36, 42, 51, 52, 54, 55, 57, 59

.......... 42 β .......... 60

.............. 80 ............ 30, 78 ............ 43, 45

.............. 46 31, 38, 49, 74,

75, 77 .............. 56 .............. 66

.............. 73 ........ 29, 65 .............. 74 ........ 69, 83 .. 37, 41, 47

→ . 31, 38, 49, 74

.......... 79 . 35, 53, 87,

89 ............ 38, 50

.............. 46 ........ 32, 81 .............. 89 .............. 44 . 58, 60, 61,

68, 79 .. 69, 83, 88 .............. 79 .............. 62 . 21, 31, 38,

49, 66, 74, 75, 77 .............. 51 .............. 85

............ 82, 84 . 31, 37, 45,

46, 48, 55, 68, 72, 75, 76

.............. 79 . 30, 52, 71,

79, 80 ........ 39, 40 .............. 44 .............. 48

............. 90 ........... 88

.............. 66 .............. 44

........... 73 .............. 39 .............. 44 ........ 33, 83 .............. 68 .............. 55 ........ 26, 67

.............. 81 → ........... 88

........ 66, 73 .. 30, 79, 80 .. 36, 61, 66

............ 46, 55 ........ 29, 65

.................. 87 .............. 66 . 31, 37, 45,

46, 48, 72, 75, 76 .............. 66

.................. 79

.. 47, 48, 49

.............. 85 ................. 40

.............. 75 .............. 48

................. 74 .............. 57 .. 47, 48, 49 . 33, 82, 86,

89 .............. 90

........ 33, 83

.............. 60 .............. 80

41, 43, 44, 45 .. 69,

88 ........ 69, 83

.......... 66 .............. 87

........... 31, 75 .............. 79 .. 36, 61, 81

.......... 51 . 57, 62, 63,

70, 76 β 53, 58, 60, 61, 68

........ 34, 50 ........ 85, 86 .............. 74 ........ 85, 86

................. 87 . 41, 43, 44,

45 . 33, 82, 86,

89 . 31, 37, 45,

46, 48, 72, 75, 76 ........ 36, 42 .............. 41

.................. 90 .............. 62 .............. 79 .............. 46 .............. 84

.. 47, 48, 49 ........... 85

2

.............. 84 ............... 85 .............. 56

.................. 76 ............ 37, 47

.............. 72 ............ 39, 40

.............. 59

........ 43, 45 ...... 24, 82, 84

........ 29, 65

........ 31, 75 .............. 41 .............. 79 .............. 85

β ........ 37, 47 .............. 67 .............. 54 .............. 68

β ........ 32, 81 ........ 34, 51 . 37, 41, 43,

47, 72 .............. 77 .............. 41

............ 34, 51 .................. 43

.............. 66

2 93 —

. 35, 36, 42, 52

.... 30, 78 .......... 62

.............. 41

............ 87, 89 ........ 30, 78

........ 19, 69 .................. 40

β .............. 64 β- ...... 76

............ 34, 51 ............ 39, 40

β .... 69, 83 .................. 87

.............. 55 .............. 81

.............. 41 .... 53, 68

........ 33, 83 ............ 36, 61

.............. 59

........ 35, 53 ........ 29, 65 .............. 60

.............. 56 ........ 35, 52

.................. 40 .............. 72

............ 36, 42 .............. 62

.................. 84 ........... 40

........ 33, 83 .............. 79 ........ 30, 80 .............. 80

.................. 79 ........ 58, 60 .............. 84

.............. 77 ............ 62, 63

.............. 81 ............ 32, 70 .................. 85

.............. 46 .............. 66 .............. 80 . 29, 39, 63,

64, 77, 78 ........... 68

.............. 81 .............. 64

. 35, 36, 42, 52, 54, 55, 86

................. 46 .............. 44 .............. 57 ........ 64, 78

α .............. 66 ................. 55

.............. 89 ........ 36, 61

.... 38, 50 .............. 89

..... 32, 47, 70

.............. 66 .............. 67

29, 63, 64, 78 .............. 42 ........ 37, 47 ........ 56, 88

................. 85

.............. 68 .............. 66

64 .............. 55 .............. 44

. 44, 57, 62, 63, 70, 76

.............. 56 → ........ 38, 49 .................. 87

........... 66 ............ 38, 50 .................. 73

........ 36, 61 .............. 58

.............. 90 .................. 67

........... 79 .............. 82

.................. 67 .............. 57

...... 55, 59, 62

.................. 58

............ 39, 40 ............ 68, 76

.............. 54 .............. 76

2 94 —

1. 本会を糸状菌分子生物学研究会（Fungal Molecular Biology Society of Japan）と呼ぶ。また本会が開

く研究会を糸状菌分子生物学コンファレンス（Conference on Fungal Genetics and Molecular Biology）と呼ぶ。

2. 本会は糸状菌の分子生物学，細胞生物学，生化学，生理学，遺伝学などの普及発展を目的とする。 3. 本会はその目的を達成するために次の事業を行う。

2. 研究会及び総会の開催。 3. 会報の発行。 4. 関連研究団体との協力事業。 5. その他，必要と思われる事業。

4. 本会はその目的に賛同して入会した個人会員及び総会において承認された名誉会員を持って構成する。 5. 本会入会希望者は所定の入会申込書を提出し，別に定める入会金を納入するものとする。 6. 本会はその運営のため，会長，運営委員若干名および会計監査 1～2 名をおく。任期は 2 年とし，改選

は運営委員の推薦と総会の承認による。 (1) 会長は本会を代表し，会務を統括する。 (2) 運営委員は運営委員会を構成し会務を審議する。運営委員には庶務，会計，編集担当，広報担当

をおく。 (3) 本会の会計事務局は会長が指名する会計担当の運営委員の所属する施設に置く。 (4) 会計監査は本会の会計を監査する。

7. 本会は事業運営に必要な実費を年会費として個人会員から徴収する。 8. 本会の事務年度は 7月 1 日から 6月 30 日までとする。 9. 前事務年度の庶務，会計については，これを総会において報告し，承認を得るものとする。 10. 本会則の改定には総会出席者過半数の賛成を必要とする。

以上 補則 (1) 本会則は 2001 年 7 月 1 日より発効する。 (2) 本会入会金は 1,000 円とする。 (3) 年会費は一般会員 2,000 円，学生会員 1,000 円とする。 (4) 研究会の通知及び会報は，当該年度までの会費を納入した会員に送付する。 (5) 2 年度にわたって会費納入のない会員は，その資格を失うものとする。 (6) 研究会の発表者は，会員に限るものとする。新入会員の演題申し込みは会費納入の確認を持って受理す

る。 （平成 23 年 11 月 16 日改正）

2 95 —

小林 哲夫 名古屋大学大学院 生命農学研究科

β

—

2 96 —

株式会社秋田今野商店 アサヒビール株式会社 天野エンザイム株式会社 イチビキ株式会社 大関株式会社 菊正宗酒造株式会社 キッコーマン株式会社 月桂冠株式会社 合同酒精株式会社 三和酒類株式会社 新日本化学工業株式会社 スパイバー株式会社 寶酒造株式会社 公益財団法人日本醸造協会 公益財団法人野田産業科学研究所 ノボザイムズ・ジャパン株式会社 白鶴酒造株式会社 株式会社ビオック ヒガシマル醤油株式会社 株式会社樋口松之助商店 ヒゲタ醤油株式会社 株式会社フジワラテクノアート マルキン忠勇株式会社 Meiji Seika ファルマ株式会社 名糖産業株式会社 ヤマサ醤油株式会社

第 15回糸状菌分子生物学コンファレンス要旨集

平成 27年 10月 26日 印刷

平成 27年 10月 26日 発行

発行者

糸状菌分子生物学研究会

編集者

山形 洋平

〒183-8509 東京都府中市幸町 3-5-8

東京農工大学大学院農学研究院応用生命化学部門