The 14tthh Conference on

Fungal Genetics
andMolecular Biology

第 14 回糸状菌分子生物学コンファレンス
2014 年 11 月 15－16 日
東北大学 川内北キャンパス

糸状菌分子生物学研究会
www.biochem.osakafu-u.ac.jp/~fmbsj/

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58'>O-1O-10? 11 % 15 $>? 12:40 - 14:40+Ȓԁ: Бͼ ď (O-1, 2)Օӷʽ П (O-3, 4)ՕŲͼ ҏ (O-5, 6)Օҝ Ć̠ (O-7, 8)Օƛ˾ ϾЕ (O-9, 10),
12:40 O-1 ՍՊё Aspergillus luchuensis S¢y·©³r±¹ӟêǇΩƳ˗S˶ЫѾˊ̒ҝ̠Օ ˕ѝ±±, ԨӻԬ, Հ˵ȵ, ǵͼĆ ՒӫІΧՓ
12:52 O-2 ϩͪёR29f²¤¹¨¢͹űɐϸҴSΑѷˡ˄мǇ 1ՕԁӴȈЕ 2Օǩ̗щʣ 1ՕͰӴǊº 1ՕԊӧʍɄ 3ՕʗǙºͿ 4Օ̯Ô͑ 5Օ΀ͼԚÇ 1 Ւ1 ͺІΧ¸͹ͧµՕ2 ͺІΧ¸|¨ɆƬՕ3 ˈŏƺ¸ӀՕ4 ͺІΧ¸ot©nu³Օ5 ˈƺ¸ʗԮƦՓ
13:04 O-3 Պё hydrophobin RolA O¥²r³ԄSΜÒöͻR29f Cys7-Cys8 ³¹Sԅ¿ͼÂɦʾ 1ՕӶĚŝ 1ՕͼӣȜ̊ 1Օ¼ŞďÑ 1ՕƺԲʭǇ 1ՕԿ˵ȵ 2ՕԊӧʍɄ 2
Ւ1 ˈŏƺԍ¸ӀՕ2 ˈŏƺԍ¸ʾˆΧՓ
13:16 O-4 ՊёϳЩȀƭjͻ/G L-2cW D-ÌӯS͹ͺϏćΛË 1ՕчÔʱ 2Օ̯Ôђ&Ǖ 2ՕяӴŒη 1Օƫ̱Ǉ 3Օι̫Ñ 3ՕӄѠʩȣ 1
Ւ1 βɓƺ¸ȀՕ2 βɓƺ¸з͞θǋՕ3 ʷ˜Ī¸ІΧՓ
13:28 O-5 ΓсаˁёRcf²z·͹İѾRȷԭQӟêǇSųǓR_9GƨΙʏĒÂ̝ǅÛ 1ՕǗǼǍǥ 2Օˀͼ¿º 1 Ւ1 Ùƺ¸ӀՕ2 ˥ˋІΧՓ
13:40 O-6 ϩͪё4ϳЩƸRİ̤Af β-¦··İѾRԅ¿AfʗѸ·yҮSѾˊӶǇęȋ 1ՕΥŞϯȤӤ 1ՕʻʷՋѪ 1ՕǵˀψË 1Օļˋ˽Ȝ 1Օƺƭ˽ʧ 1Օǩˋƃƽ 2Օȹ̒ěØ 1ՕŅѠԚƵ 1 Ւ1 Ŵƥƺ¸ӀՕ2 Ŵƺԍ¸͹žӀՓ
13:52 O-7 įцӮ̋եϩͪёNS˦ͧ-ΟёѤű·w¹S˶ЫΜѰOr´·ȺϓÂǵΟͽЕ 1,2ՕŪǿďƼӦ 3, ŲѷƉ 1, ԊӧʍɄ 1,2 Ւ1 ˈŏƺ¸ʾˆΧ, 2 ˈŏƺ¸ԍӀ¸͹ͧͺ˩Łɐ, 3 Univ. of Gothenburg, Dept. of Chemistry and Molecular BiologyՓ
14:04 O-8 Functional binding characteristics of ManR/ClrB to regulate cellulase and mannanaseproduction in Aspergillus nidulans
Nuo Li, Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi
Grad. Sch. Bioagric. Sci., Nagoya Univ.
14:16 O-9 ՊёSҸĩƔǇ FlbC TƙóƧԸͨ·ΕΑͲjίAz³}m§±¹ӟêǇՒglaBՓSΑͲjĸȯAfŲ˄ЇՕͼÂͷȃՕʗҝǫȜՕÓżŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓ
14:28 O-10 Aspergillus aculeatus R29f dipeptidyl peptidase 4 S˶ЫѾˊӓÍИƼՕƛ˾ϾЕՕҝĆ̠Օ͙ҝԬºՕǿũĽů ՒԇȐƺԍ¸͹͸θՓ 4 —

58'>O-11O-20? 11 % 15 $>? 14:50 – 16:50+Ȓԁ: ͼÂ ͷȃ (O-11~13)Օό½ ĦͿ (O-14, 15)ՕŅѠ Λ˴ (O-16, 17)Օүʽ ԣĦ (O-18~20),
14:50 O-11 Maintenance of active directional growth by perpetual assembly and disassembly of polarity sites
Norio Takeshita1,4 Yuji Ishitsuka2, Natasha Savage3, Yiming Li2, Anna Bergs1, Daria Kohler2,
Rebecca Donnelly3, G. Ulrich Nienhaus2, Reinhard Fischer1
Ւ1Dept. of Microbiology, Inst. for Applied Bioscience, 2Inst. for Applied Physics, Karlsruhe Instituteof Technology (KIT). 3Dept. of Functional and Comparative Genomics, Inst. of Integrative Biology,
Univ. of Liverpool. 4Univ. of Tsukuba, Faculty of Life and Environmental Sciences.Փ
15:02 O-12 İ̤Ӯϰ͹ͺRԅ¿Af Aspergillus nidulans SunA S˶ЫѾˊпǵ.B^ՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ¸͹žӀǋՓ
15:14 O-13 ϩͪё§}·²mS˶ЫYS·w¹ HysA Sԅ¿ˋʟϫՕǩǺɏÝՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ¸͹žӀՓ
15:26 O-14 Պё A. oryzae R29fĞýǉȾSİ͹ǇȢɐɛĸ©u¨RԅAfѾˊ
Helge M. DietrichՕͼÂŉ̑ՕӶ ӹˇՕÃǵ͒ºՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓ
15:38 O-15 u¹¤·u¤±oɛĸĸȯƔǇ CreA ṰȾŎ˅åR2/MǍǓŎAf
ͼÂͷȃՕʗҝǫȜՕÓżŌË ՒˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓ
15:50 O-16 ©µ³¢o anditomin ͹űɐSģǚѾʣˉͼûƺՕ̸ǿǊЗՕЭˀʋȍՕԊӧӥʺ Ւˈƺԍ¸џՓ
16:02 O-17 ϩͪё Aspergillus nidulans RcfƜƴ§·ӯSˬӏƷŎÂ͓ǀЕՕК̡ΧºՕԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓ
16:14 O-18 Ŏűͧm´ojͻ/G©±·͹űɐԉǘľɵϱˀǵԿȍ 1,2ՕͼÂԑǇ 2ՕԁͼѯÇ 1,2 Ւ1 ʹΧ¸ɝ͹ͧҮՕ2 ʹΧ¸CSRSՓ
16:26 O-19 p²Բ͙ΌΎёR29fįцӮ̋´ȺϓĸȯƔǇ WHI2 S£ªµz CoWHI2 TǛÄԈȯȺϓSҎǨO͉̭ͧǜ͹ȾSĸȯRԅ¿AfŞͼҬ, ÆĄȔÇ ՒÙȐƺԍ¸͹͸Փ
16:38 O-20 ¦o}po³ɊˑRcfϩͪёϳЩƲSˬӏƷŎʻʷИǇՕӷʽąȜՕύŞϴ ՒǗƥƺ¸Գͺ˩¸͸ưՕǷǵƺ¸˦ͧΧՓ 5 —

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P-1

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11 % 16 $>$? 9:30 – 10:45>#,?
10:45 – 12:00>#,?

̦ΗӱӏRͻ/dgM/fՍՊёSϪϽǋΕѾˊƮŞ˽ă 1Օ͂ÆƠʊ̘ 1Օȩ̀ʹƁ 1Օˈʧǀ 1ՕƺƥȤԩ 1Օ͂Ӣ̩α 2ՕƸǵřщ 2ՕǵͼĆ 3Ւ1 otqՕ2 ͵ͳƺӀ¸Õ͢͹ҪՕ3 ӫІΧՓP-2

Influence of light on growth and conidiation of Aspergillus oryzae
Pushpa S Murthy1, 2, Ken-Ichi Kusumoto2, Satoshi Suzuki2 Ւ1CSIR-CFTRI, India, 2NFRI, NAROՓ

P-3

ՊёІű|¨¹¡¹ՒCAoGDՓS¹¹ʳʗOESĶͻБͼď 1Օ¼˄̩ƾ 3ՕǸ½ſѯ 1,2 Ւ1 ӫІΧՕ2 ȎǺƺ¸ĝϊΧՕ3 ˗Țéΰ²Փ

P-4

ՊёSm§±¹͹ͺRԅ¿AfҸĩƔǇSŰο͙ϰ͈R29fϳЩħǯƞѾˊÜӴŢЂՕӷʽτƼՕͼÂͷȃՕʗҝǫȜՕÓżŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓP-5Պё΂Ԧ̭Ⱦ·yҮ hydrophobin RolA SΉ̒ȾѫԦYSŷΠ˶ˬSѾˊ̓ǵɂЕ 1ՕͼÂɦʾ 1ՕͼӣȜ̊ 1Օ¼ŞďÑ 1ՕԿ˵ȵ 2Օʸͼξȣ 3Օ˯ũĽȹ 3ՕԊӧʍɄ 1,2
Ւ1 ˈŏƺԍ¸ӀՕ2 ˈŏƺ¸ʾˆΧՕ3 ˈŏƺ¸ƹěΧՓP-6Պё hydrophobin RolA O¥²r³ԄSΜÒöͻR29f Cys7-Cys8 ³¹Sԅ¿ͼÂɦʾ 1ՕӶĚŝ 1ՕͼӣȜ̊ 1Օ¼ŞďÑ 1ՕƺԲʭǇ 1ՕԿ˵ȵ 2ՕԊӧʍɄ 2
Ւ1 ˈŏƺԍ¸ӀՕ2 ˈŏƺԍ¸ʾˆΧՓP-7Պё hydrophobin RolA O cutinase CutL1 ԄSΜÒöͻRԅ¿Af CutL1 Sm§ӯ̄ƨӶ Ěŝ 1, Ǣħ ѯҧ 2, ͼÂ ɦʾ 1, ǧԻ ѯҏ 1, ¼Ş ďÑ 1, Կ˵ ȵ 3, Ԋӧ ʍɄ 1,2,3Ւ1 ˈŏƺԍ¸͹ͧͺ˩Łɐ, 2 ˈŏƺ¸Ӏ, 3 ˈŏƺ¸ʾˆΧՓP-8̒ȾÑΜİө̥ՒATPSՓRcfՊё Aspergillus oryzae ͽˆ Hydrophobin HypA Sİԝ¸͕Ў¨SˬϚÂӴǐҷՕˁʘȔѯՕƪļƟòՕŅ͖ʣʜԺՕÂǺʧϲ Ւʣ̠ƺԍ¸Ӏ¸ӀŎՓP-9ϩͪёͽˆSĠ΋ƓӠ˶ЫȾ·yҮjͻ/GʗѸŐΐͻϢǇSԃΑñѠƺҧ 1, ͂ӢαӲϾ 2, ˉ˄Ժђ 2, Կ˵ɌƼӦ 3, Կ˵ȵ, ˄ƤĤщ 1, ΥÔɂǇ 2, ǿ¼ſЗ 2,ī˳ҧɐ 4, Կѷҏº 5, ԊǬԚʑ 5, δˀǋ 3, ԊӧʍɄ 1, 6 Ւ1 ˈŏƺԍӀ, 2 ˈŏƺԍŐ, 3 ˈŏƺ¸ŅՏΧ, 4 ǵȢƺʹ,5 ˈŏƺ¸ƹěΧ, 6 ˈŏƺ¸ʾˆΧՓ 6 —

P-10 Պё A. oryzae Sr±¹o·¹˭·yҮǵ½ìԙ 1, ȋˉρÅф 2, ǁ˄˺ͽ 2, ǩ˥ͽЕǇ 2, ɘΡɂº 2, ʣΥҧѯ 1, ǩǿҬÑ 3, Ñʇăω 2
Ւ1 ΓՅӫӏեΧσՕ2 ŴƥƺџՕ3ՒͫՓˈŴŪǱΎԍՓ

P-11 Պё A. oryzae R29ft¹l¹ԅӐг·yҮ AoAtg9 SѾˊѠʽОȋՕѐԄԒȹՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓP-12 ϩͪёR29f²¤¹¨¢͹űɐϸҴSΑѷˡ˄мǇ 1ՕԁӴȈЕ 2Օǩ̗щʣ 1ՕͰӴǊº 1ՕԊӧʍɄ 3ՕʗǙºͿ 4Օ̯Ô͑ 5Օ΀ͼԚÇ 1
Ւ1 ͺІΧ¸͹ͧµՕ2 ͺІΧ¸|¨ɆƬՕ3 ˈŏƺ¸ӀՕ4 ͺІΧ¸ot©nu³Օ 5 ˈƺ¸ʗԮƦՓP-13³±¹ӟêǇj¦³}¹ǨĢ?GՊёSӟêǇ}¹ʎO³±¹̭Ⱦ

чÔʱ 1Օ̯Ôђ&Ǖ 1ՕяӴŒη 2Օƫ̱Ǉ 3Օι̫Ñ 3ՕӄѠ ʩȣ 2
Ւ1 βɓƺ¸з͞θǋՕ2 βɓƺ¸ȀՕ3 ʷ˜Ī¸ІΧՓP-14 ̎Һ|§yRcfՊёS·ο·yҮԿ͹ͺRԅ¿AfƷ·ӟêǇSųǓ
ӶӹˇՕÃǵ͒ºՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓP-15 ՊёR29fz³}¹ɛĸԅӐƔǇӟêǇΩƳ˗jǛÄO?G·οӟêǇԿΑͲº͖˟ǇՕͼÂͷȃՕʗҝǫȜՕÓżŌË ՒˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓP-16 ՊёϳЩƲS α-z³u·űɐRԅifƹӳӟêǇΩƳ˗SȢɋ2cWͧҮ͹ͺͨȾȟʖˆՕͼÂͷȃՕʗҝǫȜՕÓżŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓP-17 ՍՊё Aspergillus luchuensis S¢y·©³r±¹ӟêǇΩƳ˗S˶ЫѾˊ̒ҝ̠Օ ˕ѝ±±, ԨӻԬ, Հ˵ȵ, ǵͼĆ ՒӫІΧՓ

P-18 ՊёϳЩȀƭjͻ/G L-2cW D-ÌӯS͹ͺϏćΛË 1ՕчÔʱ 2Օ̯Ôђ&Ǖ 2ՕяӴŒη 1Օƫ̱Ǉ 3Օι̫Ñ 3ՕӄѠʩȣ 1
Ւ1 βɓƺ¸ȀՕ2 βɓƺ¸з͞θǋՕ3 ʷ˜Ī¸ІΧՓ

P-19 t´o·ӯšW²¹³ӯԿ͹ͺjΚΕO?G Mortierella alpina SİǇХοԇˀՆѦ 1Օ˷ҝщ̠ 2ՕǍѠʫѸ 3ՕǺ Ϯ 4Օǩǿ Ԭ 1,3
Ւ1 ÙƺԍӀեȺͻ͹žՕ2 ȳǺƺԍեȀՕ3 Ùƺ͹ʹ®Օ4 ՐҝƺՓP-20 Pythium sp.ͽˆ ω3 ¾ԶſŎӮϰӟêǇj̭ͻ?G̟ϨȲ͹ͧ Mortierella alpina 1S-4 Rcf
EPA Sȉ̈́͹ͺǍѠʫѸ 1, 2ՕÂӂҔȋ 2ՕѐǿǠŭ 2Օ˷ҝщ̠ 3ՕǩǿԬ 1, 2
Ւ՘Ùƺ¸͹ʹŎǋ®ՕՙÙƺԍ¸Ӏ¸Ⱥͻ͹žՕ՚ȳǺƺԍ¸tՓ 7 —

P-21 ϩͪё Pythium sp. ͽˆ ω3 ¾ԶſŎӮϰӟêǇSӮ̋ΑͲϪjͻ/G˶ЫѾˊѐǿǠŭ 1ՕÂӂҔȋ 1Օ̯Ôƺҧ 1Օ˷ҝщ̠ 1,2ՕǍѠʫѸ 1,3ՕǩǿԬ 1,3
Ւ1 ÙƺԍӀ¸Ⱥͻ͹žՕ2 ȳǺƺԍ¸tՕ3 Ùƺ¸͹ʹŎǋՓ

P-22 ÛȀy´m¹ TALENs jͻ/Go/aIΎёR29fԿňͯӟêǇʇƷ̥э̼ҧÇ 1ՕǩǿƃË 1ՕƺӲĆº 1ՕñÆԄƃŭ 2Օǵˀŕ 2Օʸ̖Ń 3Օ˞ͼъ 1
Ւ1 ʣ̠ƺԍӀՕ2 ȎǺƺԍʹՕ3 ӀȀƺԍӀՓ

P-23 ̇ёľ¥²tw·НȾӟêǇSųǓ
œˀǒ 1Օ̣̬Ȝα 2Օŏįԙ͹ 1ՕͼÂŒǦ 1 Ւ1 ÙӨƺ¸ԍ¸ӀՕ2 ͍ҩΞχƺ¸͸ưθǋՓ

P-24 ˦ͧΎŞё Ustilago maydis R29fĳʼr·¹¨ŊɋS͹ʹǋΕɈЗRԅAfѾˊ˯ũѯ˹Ӧ 1, Gero Steinberg2 Ւ1 Êƺԍ¸͹Ҫ͸¸͹ž˶ЫՕ2 ry

¹ƺՕ͹žθǋՓ

P-25 pz°{SǇǕóʾɐ͡υ͞Ʒ·óSŞƔӟêǇT CHD1 £ªµzj}¹?
M/G%˄ũěՕ΃Â;B1ՕǷӴ˜˴ ՒηͼΞχƺ¸͹ͧҪ͈Փ

P-26 ͦьĥ͹ϩͪё Epichloë festucae SïİǇӵ G ·yҮ Cdc42 2cW RacA SΜÒöͻƔ
Ǉͨ·ȾS˶ЫѾˊ˫ӴŢԺՕόˀƺŸ ՒŴƺԍ¸͹žӀǋՓ

P-27 ͦьĥ͹ϩͪё Epichloë festucae R29fёϩѤű˸ɽ˗SɵϱOĥ͹έχЫSѾˊǷ˄ʑԩՕͼÂɉǇՕόˀƺŸ ՒŴƺԍ¸͹žӀǋՓ

P-28 BiFC ̥jĶͻ?GՊё A. oryzae SёϩѤűSūѹŎOѾˊǷӧ΢ȝ 1ՕƮǼſ÷Ǉ 1ՕӶ ӹˇ 1ՕǸ½ſѯ 2ՕѠÔӥԙ 3ՕÃǵ͒º 1ՕŏˀŌV; 1
Ւ1 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՕ2 ӫІΧՕ3 ԇȐƺԍ¸ʹՓP-29 Պё Aspergillus oryzae SёϩѤűR29f AoSO S˶ЫѾˊƮǼſ÷ǇՕÃǵ͒ºՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓP-30 Պё A. oryzae SǇƐЩǇȢɐR29fʸȾ͹̅ԅӐӟêǇSԿΑͲSĂӑňˌͼÂŉ̑ՕӶ ӹˇՕÃǵ͒ºՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓP-31 Investigation of the mechanism for septal association of Leashin protein in Aspergillus oryzae
Pei HAN, Feng Jie JIN, Jun-ichi MARUYAMA, Katsuhiko KITAMOTOՒDept. of Biotechnol., Univ. of TokyoՓ 8 —

P-32 Պё A. oryzae R29fĞýǉȾSİ͹ǇȢɐɛĸ©u¨RԅAfѾˊ
Helge M. DietrichՕͼÂŉ̑ՕӶ ӹˇՕÃǵ͒ºՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓP-33 u¹¤·u¤±oɛĸĸȯƔǇ CreA ṰȾŎ˅åR2/MǍǓŎAf
ͼÂͷȃՕʗҝǫȜՕÓżŌË ՒˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓP-34 ՊёR29ft¹l¹Rcf˘SİѾՒy´tl¹Փ S҈þ̥»ҝԒǐՕѐԄԒȹՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓP-35 ՊёR29f Acyl-CoA binding protein (AoAcb1, AoAcb2)Rcfͨ̃İ̤ϸҴSѾˊǿũнȋՕѐԄԒȹՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓP-36 Պё Aspergillus oryzae S¥²²·ӯáҚԅӐӟêǇS˶ЫѾˊƹͼń͹, ƺũV3f, ˨ˀɏº ՒӀΧ˶ˬ ԳІΧՓP-37 Maintenance of active directional growth by perpetual assembly and disassembly of polarity sites
Norio Takeshita1,4 Yuji Ishitsuka2, Natasha Savage3, Yiming Li2, Anna Bergs1, Daria Kohler2, Rebecca
Donnelly3, G. Ulrich Nienhaus2, Reinhard Fischer1 Ւ1Dept. of Microbiology, Inst. for Applied Bioscience,2

Inst. for Applied Physics, Karlsruhe Institute of Technology (KIT). 3Dept. of Functional and Comparative

Genomics, Inst. of Integrative Biology, Univ. of Liverpool. 4Univ. of Tsukuba, Faculty of Life andEnvironmental Sciences.Փ

P-38 İ̤Ӯϰ͹ͺRԅ¿Af Aspergillus nidulans SunA S˶ЫѾˊпǵ.B^ՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ¸͹žӀǋՓ

P-39 Aspergillus nidulans R29fµo·w¹ C Rcfu³p¨Ⱥϓz³êӘϸҴĸȯ˶ˬSѾˊͤǵͶË 1Օȹ̧ę 2ՕŲǿřʑ 3ՕƩħѯÇ 1 Ւ1 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՕ2 ǸɗŐƺ¸/iMˈŏ©nu³¸©v·y˶ˬՕ3 ˈӀƺ¸Ⱥ͹θ¸otՓ

P-40 ϩͪё§}·²mS˶ЫYS·w¹ HysA Sԅ¿ˋʟϫՕǩǺɏÝՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ¸͹žӀՓP-41 ϩͪё Aspergillus nidulans R29f²·ӯƨäÝƔǇ YpdA O´¥·´x­´¹¹
SskAՕSrrA SΜÒöͻSѾˊδԄ̩Ç 1ՕЇǿѯр 1ՕѕŞƺα 2,3ՕŪǿďƼӦ 4ՕÂǵΟͽЕ 2ՕŲѷƉ 2ՕԊӧʍɄ 1,2
Ւ1 ˈŏƺԍ¸͹ͧͺ˩ŁɐՕ2 ˈŏƺ¸ʾˆΧՕՒͲՓ3 Œїƺ¸Οё 9 —

·¹Օ4 °¹¤²ƺՓP-42 ϩͪё PKC Rͨ·ΕQʗѸԉǘľRǣAfӮ̋y²¹·zϪSʶӜŎȏůӥƾ 1ՕÂǵΟͽЕ 2ՕŲѷƉ 2ՕѠǷʰĻ 3Օ̞ű̽ 3ՕƩħѯÇ 4, ˡǵεʣ 5, ԊӧʍɄ 1,2
Ւ1 ˈŏƺԍӀ¸͹ͧͺ˩Łɐ, 2 ˈŏƺ¸ʾˆΧՕ3 y§moŎǋȀ˩, 4 ˈƺԍӀ, 6 ÂƾƺʹȀՓ

P-43 Aspergillus nidulans S wspA S˶ЫOw·űɐӮϰǯƞŎR29fȧŀo µՕʥ ̱жՕƩħ ѯÇ Ւˈƺԍ¸Ӏ͹θՓP-44 Պё Aspergillus oryzae admA, admB ӟêǇ˸ɽ˗SϳЩƲˬɐƹϧO RNA-Seq Ѿˊǩˋɦƍ 1Օļͼ̱ 1ՕŪǼĶϫ 2ՕΥÔºƽ 2Օʸ̖Ń 2Օόħӗԙ 1ՕǵȢ̫ȋ 1
Ւ1 ˈӀȀƺԍ¸Ⱥ͹θՕ2 ˈӀȀƺԍ¸ӀǋϪ|¨Û˃Хɐµz±¨Փ

P-45 Aspergillus nidulans R29fv±y±¹ҸλӮϰS˶ЫѾˊͤ̀ͽ÷Ǉ 1ՕϛƮʟϫ 2Օ̣Ǖ 2Օ̲ӴƟҼ 1Օόǿў 3ՕȫѠ˽Ķ 3ՕӴ˄Ɗȍ 1ՕǷɦÑ 1
Ւ1 ǻƥƺ¸͹ͧ͹žՕ2 Ƿǵƺԍ¸͸ư͹žՕ3 Êƺԍ¸ӀՓP-46 Չё Aspergillus oryzae S·pΑ͢ԅӐӟêǇOΜųȾjίAӟêǇSΑͲ̎ҺǩύŞřą 1Օ͂ӁԒȍ 1ՕèѠѐº 2ՕÓżŌË 3
Ւ1 ηͼΞІԳΧ

Օ2 ǸɗƺӀ¸ǟĬotՕ3 ˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓP-47 ՊёR29f Ustiloxin B ͹űɐӟêǇy±¹ҸĩƔǇ ustR ԿΑͲRcf Ustiloxin B ͹ͺŲѷƉ 1Օˡ˄мǇ 2ՕԁӴȈЕ 3Օǩ̗щʣ 2Օ΀ͼԚÇ 2ՕԊӧʍɄ 1,4
Ւ1 ˈŏƺ¸NICHeՕ2 ͺІΧ¸͹ͧµՕ3 ͺІΧ¸CBRCՕ4 ˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓP-48 ΓсаˁёRcf²z·͹İѾRȷԭQӟêǇSųǓR_9GƨΙʏĒÂ̝ǅÛ 1ՕǗǼǍǥ 2Օˀͼ¿º 1 Ւ1 Ùƺ¸ӀՕ2 ˥ˋІΧՓ

P-49 ɣǇё Phanerochaete chrysosporium ͽˆ PQQ ýǉȾӯŎӡěӮϰӟêǇSyµ¹·z2cWΑͲɓҝĞȋ 1Օˡ͓σ 2ՕΥͼŕË 1ՕŲͼҏ 2ՕÓőǽƟʜǇ 1ՕՃǺ˽̱ 1
Ւ1 ˈƺԍ¸Ӏ͹θՕ2 ӀȀƺ¸ӀՓP-50 ɣǇё Phanerochaete chrysosporium S

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u·̼Ņňˌ
ǿ˄ʰ˴ՕÂ˄ȥȣՕΥͼŕËՕÓőǽƟʜǇ, ՃǺ˽̱ Ւˈƺԍ¸Ӏ͹θՓP-51 Aspergillus oryzae ͽˆʗѸQm

³w±·r±¹SͨȴL9ƺƮƨȎՕ͂ӢѯËՕƯӴЗÛՕǩԅŕË ՒǵȢƺ¸ӀՓ 10 —P-52 ¦{ՒTricholoma matsutakeՓͽˆ³±¹ӟêǇS cDNA yµ¹·zƺ̡Ȏǔ 1Օδͼ̩Æ 1Օ˨ͼͷρ 2ՕǢ½Ԓƽ 1ՕΓơɏω 1
Ւ1 ӄΈƺԍ¸ӀȺ͹ŎՕ2 ƺԇȐƺԍ¸͹žȺ͹ŎՓ

P-53 ͨȴΕQƨҮͨ·ȾjɪKՊёͽˆʗѸ β-z³}¹(BglH)SӮϰǋΕҖȾҮ͂ӧ ʩՕӷʽ єՕȀѠ÷ӤǇՕ̐ǙɐԒՕÓżŌË ՒˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓP-54 ϩͪё4ϳЩƸRİ̤Af β-¦··İѾRԅ¿AfʗѸ·yҮSѾˊӶǇęȋ 1, ΥŞϯȤӤ 1, ʻʷՋѪ 1, ǵˀψË 1, ļˋ˽Ȝ 1, ƺƭ˽ʧ 1, ǩˋƃƽ 2, ȹ̒ěØ 1ՕŅѠԚƵ 1 Ւ1 Ŵƥƺ¸ӀՕ2 Ŵƺԍ¸͹žӀՓP-55 Պё Aspergillus oryzae SɪKİ̤ƣ££²¹ A2 SӮϰǋΕȾҮSѾˊԿ˓ÕͽЕ 1, ǗǿɦË 2, ƺƮ̺ 2, ͼÇćę 2, ŏˀŌV; 1, ʸǷǋ 1
Ւ1 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՕ2 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹ŎՓP-56 ՌՊё Aspergillus oryzae pepO ӟêǇ˸ɽ˗SёóƸr·ƣµm¹RK/M¼ӴϻǇ, ļͼ̱, ǵȢ̫ȋ, όħӗԙ ՒӀȀƺԍ¸Ⱥ͹ŎՓP-57 Emericella variecolor R29f

³¢·űɐӮϰSɵϱ»˵ԒωՕˉͼûƺՕ̸ǿǊЗՕԊӧӥʺ Ւˈƺԍ¸џՓP-58 o{(Lentinula edodes)R29f GABA ͹ɐRԅ¿AfӮϰRK/MǸˀſǇՕδͼ̩ÆՕΓơɏω ՒӄΈƺ¸Ӏ¸Ⱥ͹ŎՓP-59 ·Qf̈́ȑNƧԸ?G Aspergillus fumigatus ЩǇS̎Һ±·y²¹¨ѾˊѕŞƺα 1ՕӫÔԺǀ̖ 1ՕӷʽП 2ՕÍÔğȣ 1ՕÓÔӋ 1Օǿˀӑ 1
Ւ1 Œїƺ¸Οё·¹Օ2 ԳІΧՓP-60 ΓՊёR29fɷǓҸĩĸȯƔǇ NosA O RosA SѾˊÑβ̩ƨ 1Օͼáʰŭ 2ՕˤŞȔř 3ՕԿ½εʧ 3Օόǿў 2ՕͰГǫȳ 1ՕȫѠ˽Ķ 2
Ւ1 ՇġǺƺ¸ӀՕ2 Êƺԍ¸ӀՕ3 »ſӫԲՓ

P-61 ӸȿȉȾRԅifҸĩƔǇ HapX O CCAAT-box ϹűƔǇ HapB/C/E OSΜÒöͻÂ˄ԘÛՕӶǇęȋՕȹ̒ěØՕŅѠԚƵ ՒŴƥƺǋ¸ӀǋӧՓP-62 ՊёSҸĩƔǇ FlbC TƙóƧԸͨ·ΕΑͲjίAz³}m§±¹ӟêǇՒ glaBՓSΑͲjĸȯAfŲ˄ЇՕͼÂͷȃՕʗҝǫȜՕÓż ŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓ 11 —P-63 Aspergillus oryzae ҸĩƔǇ XlnR/AraR RcfҸĩĸȯ˶ˬSѾˊΥǿԺŗՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ͹žӀ¸͹ͧ˶ˬՓ

P-64 Functional binding characteristics of ManR/ClrB to regulate cellulase and mannanase production in
Aspergillus nidulans
Nuo Li, Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo KobayashiՒGrad. Sch. Bioagric. Sci., Nagoya Univ.Փ

P-65 Պё¦³¹ҪŎӟêǇy±¹Sm§±¹ҎǨ͹ͺYSԅ¿ȆǿʠĦՕԁҝǿՖƥγǇՕͼÂͷȃՕʗҝǫȜՕÓżŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓP-66 ՌՊё Aspergillus oryzae pepO ӟêǇS cis-element SɵϱǵǼŻȋ, ļͼ̱, όħӗԙ, ǵȢ̫ȋ ՒӀȀƺԍ¸ӀՓP-67 ϩͪё Trichoderma reesei Sm±x·ӯµm¹SΑͲҎǨ˶ˬSѾʣƯǱȍ˴ՕԟΟȜՕñѠʧђՕȹͼ̫Ý, ǩύŞ̿ ՒԁǷəθƺ¸͹ͧՓP-68 Aspergillus nidulans

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P-69 ±·¥¹¹ʇƷRcf}pӯSƺӵ͹ͺñӴěʩ, ŏǿ̠ɂ, ƺϘąº ՒӶ̝ȀƺՓ

P-70 ՊёSr³~µ¹³͹űɐjĸȯAfҸĩƔǇ AtrR O SrbA S˶Ы2cWϳЩħǯƞѾˊ˂ǵнȋՕƺƭ˿ՕѕŞƺα 1ՕͼÂͷȃՕʗҝǫȜՕǿˀӑ 1ՕÓżŌËՒˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՕ1 Œїƺ¸Οё·¹Փ

P-71 Aspergillus nidulans S sirtuin moo¨RcfÑ˹áҚϪSΑͲĸȯèѠщӲǇՕъˀÚҼՕˠǭăÝՕԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓ

P-72 ՌՊё²·ou³¤w¢¹ӟêǇR29fo·µ·̄ǉȾSѾˊΥͼď, ÆĄǺɂ, ˥ͼǠÛ, ļͼ̱, ǷˀЄǇ, όħӗԙ, ǵȢ̫ȋ ՒˈÙӀȀƺ¸Ⱥ͹θՓP-73 Aspergillus oryzae R29f 331-25 sense RNAՕ331-25 antisense RNA S˶ЫѾˊӂÔԚՕǁͼПՕόħӗԙՕǵȢ̫ȋ ՒˈÙӀȀƺ¸Ⱥ͹θՓP-74 Aspergillus aculeatus R29f dipeptidyl peptidase 4 S˶ЫѾˊӓÍИƼՕƛ˾ϾЕՕҝĆ̠Օ͙ҝԬºՕǿũĽů ՒԇȐƺԍ¸͹͸θՓ 12 —P-75 Aspergillus oryzae Soµs¹·ЖS˶Ы2cWǯƞȾSѾˊʟǿуòѓ, ΥͼŒϾ, ǵǿϹ, Œáę, ÂǺʧϲ Ւʣ̠ƺԍ¸Ӏ¸ӀŎՓ

P-76 įцӮ̋եϩͪёNS˦ͧ-ΟёѤű·w¹S˶ЫΜѰOr´·ȺϓÂǵΟͽЕ 1,2ՕŪǿďƼӦ 3, ŲѷƉ 1, ԊӧʍɄ 1,2 Ւ1 ˈŏƺ¸ʾˆΧՕ2 ˈŏƺ¸ԍӀ¸͹ͧͺ˩ŁɐՕ3 Univ. of Gothenburg, Dept. of Chemistry and Molecular BiologyՓ

P-77 Fusarium graminearum 2cW Fusarium sporotrichioides R29fҸĩƔǇ TRI6 S˶ЫÒɺȾÂǾòºՕļͼºѦՕӶÃÙǇՕǩˋƃƽՕʽ˄Ο ՒŴƺԍ¸͹žӀՓP-78 ϩͪё Trichoderma reesei R29f pH ýǉΕ

³±¹͹ͺ©u¨SѾˊȋ̝ƺ˴ՕƯǱȍ˴Օȹͼ̫ÝՕǩύŞ̿ ՒԁǷəθƺ¸͹ͧՓ

P-79 ϩͪё Trichoderma reesei S³±¹͹ͺĸȯƔǇSЃДΕѾˊéͼǐ˴ՕƯǱȍ˴Օȹͼ̫ÝՕǩύŞ̿ ՒԁǷəθƺ¸͹ͧՓP-80 oθ˦ͧ/aIΎёS Argonaute3 T RNA o´··zjҡRĸȯAf
ĢҝȥщՕ˲Ρ÷ǀՕÂǱʐƢ Ւβɓƺԍ¸ӀՓP-81 ХοYSȺͻjΚΕO?Go{|¨өĲʏĒơˀѯº, ñѠȹρՕӶǇΟË 1Օ̯Ӵ=O^ 1ՕǗǼǍǥ 2ՕΓΥӑ 3ՕǗǼſȜ 2ՒǸɗ͹ȀΧՕ1 ˈȀƺ¸͹žʹȀՕ2 ˥ˋІΧՕ3 Êƺ¸ӀǋΧσԍՓ

P-82 ©µ³¢o terretonin ͹űɐ˶ˬSѾʣ2cWԅӐĆԷӮϰЖS˶ЫѾˊǸ̀ƺҽՕˉͼûƺՕ̸ǿǊЗՕԊӧӥʺ Ւˈƺԍ¸џՓP-83 ©µ³¢o anditomin ͹űɐSģǚѾʣˉͼûƺՕ̸ǿǊЗՕЭˀʋȍՕԊӧӥʺ Ւˈƺԍ¸џՓP-84 Emericella variecolor ͽˆʗѸ©µ³¢o͹űɐӟêǇy±¹S˶ЫѾˊģʰɹՕˉͼûƺՕ»˵ԒωՕԊӧӥʺ Ւˈƺԍџ¸ƻͧ͞ŎǋՓ

P-85 Penicillium purpurogenum R29f Monascus сϰ͹űɐԅӐ¥²{͹űɐӟêǇSɵϱяŞ̺ՕǩǾ̷ՕъʽЕ˴ՕՎѠÚՕʗǰӸȋՕŅѠԬՕʧѷԒʑ Ւʜƺ¸͹ͧҪ͈¸͹žŎǋՓ

P-86 ϩͪё Aspergillus nidulans RcfƜƴ§·ӯSˬӏƷŎÂ͓ǀЕՕК̡ΧºՕԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓ 13 —P-87 ozµ¦o· B ĮʹRcf³±yr·͹ͺϩͪё Fusarium sp. RK97-94 R29fÑ˹áҚͺͧ͹ͺҎǨŅѠИ 1,2, ˀǵԿȍ 1,3ՕӽćԿȹ 2, ԁͼѯÇ 1,3 Ւ1 ʹΧ¸ɝ͹ͧҮՕ2 ˈÙʹθƺՕ3 ʹΧ¸CSRS,Փ

P-88 rw

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· A YSƷɺRԅifӮϰӟêǇSɵϱŅѠΛ˴ 1ՕJae-Hyuk JANG2ՕԿ˵ăÑ 1ՕJong Seog AHN2ՕԁͼѯÇ 1 Ւ1 ʹΧ¸CSRSՕ2KRIBBՓ

P-89 Aspergillus nidulans SïӯϰҎǨȾЯ®w·ŎӮϰS˶ЫԊӧƾѦՕˠǭăÝՕԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓ

P-90 Պёm³ CoA űɐӮϰ˸ƿ˗RcfӓԝЬФӯSԿ͹ͺͰӴǊº 1ՕKenneth S. Bruno2Օǩ̗щʣ 1ՕΥÔʰǇ 1Օ»̰ɉ 1Օǵ˙ČǇ 1Օˡ˄мǇ 1ՕScott E.
Baker2Օ΀ͼԚÇ 1 Ւ1 ͺІΧ¸͹ͧµՕ2 ϟƚny¹prƚχΧσɕՓ

P-91 o/aIΎёS Ehs1 SympՕyp·R29fѫͲƣS̎ҺO˹Àá¹{·¹Rcf±·y²¹¨Ѿˊ˄ӴɎǀՕȖ͓ɦȄՕɐǿɂՕэ̼ҧÇՕʗÔſрՕƺԀ͒Օ˞ͼъՕӽćԿȹՒˈʹƺԍʹȀ¸Ⱥ͹θՓP-92 Ŏűͧm´ojͻ/G©±·͹űɐԉǘľɵϱˀǵԿȍ 1,2ՕͼÂԑǇ 2ՕԁͼѯÇ 1,2 Ւ1 ʹΧ¸ɝ͹ͧҮՕ2 ʹΧ¸CSRSՓ

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SpecialLecture)8'

Molecular dissection of galactofuranose biosynthesis in Aspergillus
niger and its importance for maintaining cell wall integrity
Arthur F. J. Ram1, Joohae Park1, Boris Tefsen2,, Ellen Lagendijk1, Cees A.M.J.J. van den
Hondel1, Irma van Die2, Mark Arentshorst1
1

Leiden University, Institute of Biology Leiden, Molecular Microbiology andBiotechnology, Sylviusweg 72, 2333 BE Leiden, The Netherlands
2
Department of Molecular Cell Biology and Immunology, VU University Medical Center,van den Boechorststraat 7, 1081 BT, Amsterdam, The Netherlands
Abstract
The biosynthesis of cell wall galactofuranose (Galf) containing glycostructures suchas galactomannan, N-glycans, O-glycans and glycosylinositolphosphoceramides infilamentous fungi are important to secure the integrity of the cell wall. In A. niger, theabsence of Galf synthesis results in activation of the cell wall integrity (CWI)-pathway.
Previous work in our group has shown that activation of the CWI-pathway is characterized
by the induced expression of the agsA gene, which encodes a cell wall alpha-glucan
synthase. The induced expression of agsA in response to cell wall stress was used in a
genetic mutant screen to isolate cell wall mutants with a constitutive expression of agsA. In
total 240 cell wall mutants were isolated and from this mutant collection the first Galf
mutant was identified. Characterization of this mutant showed that the mutant is defective inthe ugmA gene which encodes a UDP-galactopyranose mutase which is essential for theformation of Galf (1).
To identify additional mutants defective in Galf biosynthesis, the collection of cellwall mutants was screened for the absence of Galf containing glycoconjugates in the growth
medium using an anti-Galf antibody. From the collection of mutants, we identified seven
Galf deficient mutant from which six belonged to the ugmA complementation group and one
mutant belonging to a new complementation group. By using whole genome sequencing
approach, twenty one SNPs in coding regions were identified between this new mutant andits parental strain. The mutation responsible for the Galf phenotype was found be in theugeA gene. The ugeA gene encodes a putative UDP-glucose-4-epimerase (UgeA) and ugeA
is required for the biosynthesis of Galf as well as for galactose metabolism in A. niger (2).
The addition of Galf-residues to galactomannan, galactomannoproteins andglycolipids is carried out in the Golgi apparatus by Galf transferases. UDP-Galf is producedin the cytoplasm and a nucleotide sugar transporter is required to transport UDP-Galf fromthe cytosol to the lumen of the Golgi. Such a specific member of the nucleotide sugartransporter family has recently been identified in both A. fumigatus and A. nidulans (3,4).
 16 —Based on homology searches, we identified two putative UDP-Galf-transporters in A. niger.
Deletion analysis of the single and double mutants indicate that the two putative
UDP-Galf-transporters have a redundant function in UDP-Galf-transport as only the double
mutant displayed a Galf negative phenotype. Localization of fluorescently-labeled Ugt
proteins confirmed their predicted localization in the Golgi. The Galf transferase (GfsA)
responsible for the attachment of Galf-residues to glycostructures have recently been
identified in A. fumigatus and A. nidulans (5). A. niger contains three genes that are highly
homologous to gfsA in the two other Aspergillus species.. Systematic deletion analysis of
the gfs homologs in A. niger showed that deletion of gfsA results in strong reduction in Galf
containing structures and minor roles for gfsB and gfsC.
In A. niger, the absence of Galf synthesis results in activation of the cell wall
integrity (CWI)-pathway indicating that the Galf biosynthesis is important for maintaining
cell wall strength. To identify genes involved in maintaining cell wall integrity in responseto the absence of galactofuranose biosynthesis, a genome-wide expression study was
performed with the ugmA deletion strain. RNAseq analysis revealed 250 genes to be higher
expressed in the ugmA mutant compared to the wild-type and these genes encode enzymes
involved in chitin synthesis (gfaB, gnsA, chsA), alpha-glucan synthesis (agsA), beta-glucan
remodeling (bgxA, gelF, and dfgC) and several (GPI)-anchored cell wall protein encoding
genes. Interestingly, also the gene encoding the CWI-specific Map-kinase-kinase (MkkA)
was induced in the ugmA mutant. In silico analysis of the 1-kb promoter regions of thedifferentially up-regulated genes in the ugmA mutant using an in house developed
transcription factor binding site finder program, indicated overrepresentation of genes with
RlmA or SteA binding sites. The importance of the RlmA and SteA transcription to
induce cell wall remodelling genes is currently under investigation by constructing arlmA-ugmA and steA-ugmA double mutants.
References:(1) Damveld RA, Franken A, Arentshorst M, Punt PJ, Klis FM, van den Hondel CA,
Ram AF. A novel screening method for cell wall mutants in Aspergillus niger
identifies UDP-galactopyranose mutase as an important protein in fungal cellwall biosynthesis. Genetics 2008, 178:873-881.
(2) Park JP, Tefsen B, Arentshorst M, Lagendijk E, van den Hondel CAMJJ, van Die I,
Ram AF. Identification of the UDP-glucose-4-epimerase required for
galactofuranose biosynthesis and galactose metabolism in A. niger. Fungal
Biology and Biotechnology 2014, in press(3) Engel J, Schmalhorst PS, Dörk-Bousset T, Ferrières V, Routier FH. A single
UDP-galactofuranose transporter is required for galactofuranosylation in
Aspergillus fumigatus. J Biol Chem. 2009, 284:33859-33868.
 17 —(4) Afroz S, El-Ganiny AM, Sanders DAR, Kaminskyj SGW. Roles of the Aspergillus
nidulans UDP-galactofuranose transporter, UgtA in hyphal morphogenesis, cellwall architecture, conidiation, and drug sensitivity. Fungal Genet Biol 2011,
48:896-903.
(5) Komachi Y, Hatakeyama S, Motomatsu H, Futagami T, Kizjakina K, Sobrado P,
Ekino K, Takegawa K, Goto M, Nomura Y, Oka T. GfsA encodes a novel
galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen
of O-glycan in Aspergillus nidulans and Aspergillus fumigatus. Mol Microbiol
2013, 90:1054-1073.

 18 —







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 19 —ʑͬ
1: Shoji H, Sugimoto T, Hosoi K, Shibata K, Tanabe M, Kawatsura K. J Biosci Bioeng. 2007; 103:203-205.
2: Sugimoto T, Horaguchi K, Shoji H. J Ind Microbiol Biotechnol. 2011; 38: 1985-1991.
3: Masuda S, Shoji H. J Inst Brew. 2012; 118: 346-351.
4: Sunagawa T, Masuda S, Shoji H. J Agric Sci Technol. 2014; 4: 13-26.

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The Novel Hair Dyeing Technology by Aspergillus Tyrosinase.
Yukihiro Nakamura and Yoji Hata (Research Institute, Gekkeikan Sake Co., Ltd.) 23 —S-3ƧƠŞʔՒЯЬǩՈШцՓ±o¬¹Sә/Rcf
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1: yµ²¨ՒTacrolimus,FK506ՓSȀ˩ŎΧσ  ͹ͧȀǋéҌ ώ76ȅ ώ9Ů 389-397.1998
Production Inhibition for FK506 (Tacrolimus) Caused by Culture Medium (defatted wheat germ) of Different
Suppliers and Its Prevention
Ayako Futase, Ayana Ide,Kuniharu Watanabe,Shiho Shimizu(Astellas Pharma Tech Co., Ltd, Toyama Technology Center, Technology Development) 24 —S-4¤o¨ΰR29fmz²ot:ͲͪOÜȫSŦeϷ^RK/MՀʽ ȸ¤o¨ «·˗Țéΰ ΧσԃΑӧԂ
2000 ȌR 61 ĘÛO/igGÀ΂ÛũTͲƞANR 70 ĘÛjҲ1ՕʶӄSÏͅNT 2050
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M/f%ʨȌʿRTՕˀmz²ot(BioAg)jºǴӑ`fG`ϟƚª··ΰOɸɿAf;Oj̙Ǔ?G%Ӏ˩İӴNǕЏS.fª··ΰOɸɿAf;ORceՕΰéSɪЁΕΑǲRҢͬN5fot²­¹¯·jӀ˩İӴRɧƺN5f;Ojʼȩ?M/f%ÜƓTՕϩͪёjͻ/G²·ӯŷťĂӑľ 3) JumpStart®Օ˙Ϣёͽˆ Nod ƔǇjĶͻ?GöͧťӵĂӑľ 4) TagTeam®LCO QPșΰѱƀSϵÝj×1Q4dՕ¤o¨ΰR29fmz²otSŦeϷ^RK/MϵÝAf%țͻʑͬ
1: ІŋΝϽҁǯ À΂SϽҁ2014 http://www.stat.go.jp/data/sekai/0116.htm
2: USDA: Agricultural Outlook,
3: Kucey, R.M.N. 1987. Appl. Environ. Microb. 53:2699-2703.
4: PCT patent application WO2008085958
Introduction of BioAg business at Novozymes
Shinobu Takagi(R&D, Novozymes Japan Ltd.) 25 —







Oral SessionO-1 (P-17)
ՍՊё Aspergillus luchuensis S¢y·©³r±¹ӟêǇΩƳ˗S˶ЫѾˊ̒ҝ̠Օ˕ѝ±±, ԨӻԬ, Հ˵ȵ, ǵͼĆՒӫІΧՓ ͟ӪѱӏՕͨRŞʔRтjͻ/GƭűRՕȲӵS©¹³4Ŷ]gM?]0;O4ϸԽ¼΢dgM/f%͟ӪS©¹³͕ȑR2/MՕi4ƚSԳƀѨ͹̥NTѱƀ.Ge 1,000 mg/L ʾ͇O=gM2eՕģ7ƈ
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M/f% ͟ӪՊё (A. luchuensis) S|¨¹¡¹ceՕA. oryzae S PmeA OΜųȾjίAӟêǇjѷį?Օ
pmeA, B, C OžŴ?G%;gdӟêǇS©¹³͹ɐ̭ȾғZGO;hՕPmeA, B R2/MՕ¢y·jƨҮO?M©¹³͹ɐ̭Ⱦjʸ?M/fÐ4ʣd3OQJG%]GՕpmeA, pmeB SŘͫΩƳšWÑӳΩƳjѦ/Օ©¹³͹ɐ̭ȾjғZGϹˌՕpmeA jΩƳAf;ONѻ˗O̎Һ?MՕʸɈŔǪAf;Ojѷį?G%Ё/MՕǕԕSт͟ӪR2/Ma©¹³4ḯŎ=gf3jʣd3RAfG`RՕŰΩƳ˗SϟՊjͻ/Gт͟ӪǩÞӃ^҉ԽjѦJG%ESϹˌՕŰΩƳ˗ՊNӱӏ?Gт͟ӪSr¹³͕ȑTѻ˗O[\ųϑN.JGSRǣ?Օ©¹³͕ȑT pmeA ŘͫΩƳ˗šW pmeApmeB ÑӳΩƳ˗N
ƺ57́ǪAf;O4ʣd3OQJG%
Characterization of the deletion mutants of pectin methylesterase genes in Aspergillus luchuensis.
Osamu Mizutani, Dararat Kakizono, Jin Shun, Toru Takahashi, Osamu Yamada (NRIB)

O-2 (P-12)
ϩͪёR29f²¤¹¨¢͹űɐϸҴSΑѷˡ˄мǇ 1ՕԁӴȈЕ 2Օǩ̗щʣ 1ՕͰӴǊº 1ՕԊӧʍɄ 3ՕʗǙºͿ 4Օ̯Ô͑ 5Օ΀ͼԚÇ 1 Ւ1 ͺІΧ¸͹ͧµՕ2 ͺІΧ¸|¨ɆƬՕ3 ˈŏƺ¸ӀՕ4 ͺІΧ¸ot©nu³Օ5 ˈƺ¸ʗԮƦՓpµw· B T˦ͧΎŞёN.f Ustilaginoidea virens RcJMͺ͹=gf;O4΢dgf¢ȾSÑ˹áҚͧҮNՕTyr-Ala-Ile-Gly (YAIG)3dQf͸ͪ¢Rԥ²¤¹¨Ⱦm§ӯN.f³²·4ĆԷ=gGˬӏjɪK%;Sȑ Aspergillus flavus R2/Mapµw· B 4ͺ͹=gf;Ojѷį?Օ
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Q²¤¹¨¢͹űɐϸҴN.fՒRiPS ϸҴOAfՓ%A. flavus R29fpµw· B S͹űɐӟêǇy±¹T 15 ĈSӟêǇ3dQf%ESŰ&SΩƳ˗jöɐ?ՕͨȴΕRњςAfáҚÂԄójѾˊAf;ONՕ͸ͪŎRȷԭQӟêǇϑ4ʣd3RQeKK.f%EgdSϹˌRK/MƬźAf%Umemura et al., Fungal Genetics and Biology, 68: 23-30 (2014); ˀΧσTՕϸ̾ͺ˩ΝǄ҃Ð˩'ԧʗΕot¦
²m³ǕͲSG`SԿ˶ЫŎ|¨o·əѧԃΑ(SºӧO?MǕʙ=gG%
Discovery of novel ribosomal peptide biosynthetic pathway in filamentous fungi
Myco Umemura1, Nozomi Nagano1, Hideaki Koike1, Koichi Tamano1, Keietsu Abe2, Kazuo Shin-ya1, Kiyoshi Asai3,
Masayuki Machida1(1AIST, 2Tohoku Univ., 3Univ. Tokyo) 26 —O-3 (P-6)Պё hydrophobin RolA O¥²r³ԄSΜÒöͻR29f Cys7-Cys8 ³¹Sԅ¿ͼÂɦʾՒˈŏƺԍ¸ӀՓՕӶĚŝՒˈŏƺԍ¸ӀՓՕͼӣȜ̊Ւˈŏƺԍ¸ӀՓՕ¼ŞďÑՒˈŏƺԍ¸ӀՓՕƺԲʭǇՒˈŏƺԍ¸ӀՓՕԿ˵ȵՒˈŏƺԍ¸ʾˆΧՓՕԊӧʍɄՒˈŏƺ¸ʾˆΧՓhydrophobin TϩͪёRȎ7Ąǉ=gM/f΂Ԧ̭Ⱦ·yҮN.eՕ8 KSĄǉ=gG Cys ̄ƨjɪK%
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Af%RolA T PBSA RŷΠ?GȫˬӏƷŎ?ՕCutL1 j²y³¹Af;ON PBSA İѾjĂӑAf%
ˀΧσR2/MՕɑ&T PBSA YS RolA ŷΠwnyjՕ³p·m ošW Quartz Crystal
Microbalance(QCM)RcJMѾˊ?G%]GՕRolA SΉ̒Ⱦ³¹ÂRǉƞAfΉ̒Ⱦm§ӯ̄ƨjՕѻ̒Ⱦm§ӯS Ser RГɺ?GƷ·ójöѱ?ՕPBSA RǣAfŷΠwnyjѾˊ?G%Cys7-Cys8 ³¹
ÂS Leu137, Leu142 jГɺ?G RolA Ʒ·óNTՕӴ͹ƣ RolA O̎Һ?M PBSA YSŷΠӎȑ]GTʶƺŷΠӵ4ï½?G;O3dՕ;S 2 KS̄ƨ4 PBSA YSŷΠRӳѵN.eՕCys7-Cys8 ³¹4ŷΠRÄ
Rԅ¿Af;Ojίƅ?G%ͲƞՕCys7-Cys8 ³¹ÂSюԠȾm§ӯjΉ̒Ⱦm§ӯN.f Ala RГɺ?GƷ·ójͻ/ՕCys7-Cys8 ³¹ÂRǉƞAfюԠ4 PBSA YSŷΠRš\AȦԪjғZM/f%
Involvement of C7-C8 loop of Aspergillus oryzae hydrophobin RolA in interaction between RolA and a polyester.
Takumi Tanaka (Grad. Sch. Agric. Sci., Tohoku Univ.), Yoonkyung Kim (Grad. Sch. Agric. Sci., Tohoku Univ.),
Hiroki Tanabe (Grad. Sch. Agric. Sci., Tohoku Univ.), Kenji Uehara (Grad. Sch. Agric. Sci., Tohoku Univ.), Toru
Takahashi (NICHe., Tohoku Univ.), Keietsu Abe (NICHe., Tohoku Univ.).

O-4 (P-18)
ՊёϳЩȀƭjͻ/G L-2cW D-ÌӯS͹ͺϏćΛË 1ՕчÔʱ 2Օ̯Ôђ&Ǖ 2ՕяӴŒη 1Օƫ̱Ǉ 3Օι̫Ñ 3ՕӄѠʩȣ 1Ւ1 βɓƺ¸ȀՕ2 βɓƺ¸з͞θǋՕ3 ʷ˜Ī¸ІΧՓ)ΚΕ*ˀΧσSΚΕTՕՊё Aspergillus oryzae jͻ/G··3dS L-2cW D-ÌӯS͹ͺN.f%ÌӯTՕȭˆS±yϑRʵifot±yN.f¥²ÌӯSŞʔOQf%L óO D ó4̻
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g/L ··3d 23 g/L S D-Ìӯj͹ͺ?G%͹ͺ=gGÌӯSĞǋϮȑTՕ99.9%â¼4 D óN.JG%
â¼Օ Պёjͻ/f;ON··3dS L-2cW D-ÌӯS͹ͺRɐń?G%ºʘNՕES͹ͺӵTz³}¹3dS͹ͺӵO̎ZMï/%ÜȫTՕáҚʇƷϑRce͹ͺňͯSŵ¼jΚɫAOĥRՕ··
H93dNQ7 ³µ¹ot¦3dS L-2cW D-Ìӯ͹ͺjΚɫA%
Production of L- and D-lactate in Aspergillus cell factory
Naoya Sasakura1, Satoshi Wakai2, Nanami Asai2, Chiaki Ogino1, Hiroko Tsutsumi3, Yoji Hata3, Akihiko Kondo1(1Dept. Chem. Sci. Eng., Grad. Sch., Kobe Univ., 2Org. Adv. Sci. Tech., Kobe Univ., 3Res. Inst., Gekkeikan) 27 —O-5 (P-48)
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˗R 1 ˗SŀűNƨҮЯс¾ģj5GAυ͞Ʒ·ó4ĨͲc7İԝN5G՗˹RՕPC9¸PC15 ԄR29fͨ
ǓS|¨өĲȂ·jՕPCR RcJMϝĀ3KňͯΕRқĵN5fǕԽϪjέχ?G՗F1 İˊR2/MՕƷ·ѫͲƣ4ŘºӟêǇSƷ·RұƔAfOίƅ=gGυ͞Ʒ·ó B84PC15 ԄS F1 ǇǌԛƕjՕ¼҄ PCR
RcfӟêѾˊRü?G՗ϹˌՕͨǓS|¨ԮƦ4ՕƷ·ѫͲƣOȠ7ӐӾ?Mİө=gf;Ojѷ/H?GՒPC9PC15 NTՕE0NTQ3JGՓ՗â¼jҵ]1MͲƞTՕ|¨¸²¹{·jӍ@GƷ·ϕɕSͨǓՕE?MɷǓƷ·ӟêǇSΜѰǕԽRcJMՕŞƔƷ·ӟêǇjͨǓAf;Oj҉^M/f՗
Forward Genetics in the white-rot fungus Pleurotus ostreatus: Towards understanding molecular mechanisms
underlying wood decay
Takehito Nakazawa1, Yasumasa Miyazaki2, Yoichi Honda1 (1Kyoto Univ., 2FFPRI)

O-6 (P-54)
ϩͪё4ϳЩƸRİ̤Af β-¦··İѾRԅ¿AfʗѸ·yҮSѾˊӶǇęȋ 1ՕΥŞϯȤӤ 1ՕʻʷՋѪ 1ՕǵˀψË 1Օļˋ˽Ȝ 1Օƺƭ˽ʧ 1Օǩˋƃƽ 2Օȹ̒ěØ 1ՕŅѠԚƵ 1 Ւ1 Ŵƥƺ¸ӀՕ2 Ŵƺԍ¸͹žӀՓ[ΚΕ] β-¦··T˭&Q˦ͧRŶ]gfԞİѾȾƹϧNՕʾĶͻot¦SºKN.fG`Օotr
¹³SŞʔQPO?M̨Κjԛ`M/f%ɑ&TՕβ-¦··S^jƆºS͙ϰ͈O?MϩͪёAspergillus nidulans j͹Х=CGԕRՕendo-1,4-β-¦·¹OĥRϳЩƸRƹӵR͹ͺ=gf˶Ыʾ΢·yҮՒHPՓjųǓ?G%HP T!q)mb
{ek_wgdyx&~u |l]o`ji%ˀΧσNTՕϩͪёRcf β-¦··İѾR29f HP Sȧŀjʣd3RAf;OjΚΕO?G%[Ϲˌ2cWЛǡ] hp +" (ΔHP ) {'eβ-{ q#mei
l%dhimcz,m*ek%adyi\on{ q#mei,m p
%eicm`wHP rβ-q(p-fxm$^wyi\tiϦѱ?G_vs~ }q
HP {]k(eimczHP TՕ|³Ŏ?G β-¦··SÄӾjŅ̒İѾCBR β-¦··̶͋SϤȑjƺ57ï½=CG%=dRՕHP O endo-1,4-β-¦·¹j̻űAfOՕβ-¦·¹Rcf β-¦··SİѾ4Ăӑ=gG%;gdS;O3dՕHP T β-¦··İǇԄS̒ϰϹűjıʕ?ՕАЂˬӏjЋ`fė5jɪKry··˭S˶Ыjʸ?M/f;O4Л1dgG% ˀΧσSºӧT͹Χ ·¹'o¡¹¯·ŁįƨήΕΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%
Novel protein involved in β-mannan degradation from filamentous fungus Aspergillus nidulans
Yuhei Kaneko՘, Saaya Ishihara՘, Mai Mochizuki՘ Tatsuya Yamamoto՘, Masahiro Maebayashi՘, Masaharu Ohba՘,Tetsuo Kobayashiՙ, Motoyuki Shimizu՘, Masashi Kato՘ (՘Meijo Univ., ՙNagoya Univ.) 28 —O-7 (P-76)
įцӮ̋եϩͪёNS˦ͧ-ΟёѤű·w¹S˶ЫΜѰOr´·ȺϓÂǵΟͽЕ 1,2ՕŪǿďƼӦ 3, ŲѷƉ 1, ԊӧʍɄ 1,2(1 ˈŏƺ¸ʾˆΧ, 2 ˈŏƺ¸ԍӀ¸͹ͧͺ˩Łɐ, 3 Univ. of Gothenburg, Dept. of Chemistry and Molecular BiologyՓ ˦ͧSµoR2/MՕr´· ·¹O?M˶ЫAf AtETR1 T·w¹(HK)̭
ȾjɪIՕr´·RcJMES HK ̭Ⱦ4ĸȯ=gf%ˀΧσNTՕ;S˦ͧͽˆSr´·Ϲű©o·OӮ̋ƆºS HK N.f ScSln1p 2cWӮ̋NS HK ˶ЫΜѰ4ҍ`dgM/fϩͪё HK S AnTcsB RŅ
1Օ̴ӋƝɊŧRԅāAf AnNikA S·w¹©o·OѤű?G HK jEgFg҅ҁ?Օr´·ȺϓȾS HK R˶ЫʇƷ?GİǇSӏɐj҉^ՕӮ̋¸ϩͪёNS HK ˶ЫΜѰȾOr´·ȺϓȾR
K/M˧҇?G%;g]NRįцӮ̋ Sln1p ̈́ȑɊŧȾ˗R2/M ScSln1p S˶ЫΜѰȾj҈þ?GϹˌՕ
ScSln1p 2cW AnTcsB SѤű HK 4 ScSln1p S HK ̭ȾjΜѰAf;Ojέҍ?G%]GՕѤű HK jǨĢ?G˗NTr´·ĮʹN͹ХSɛĸO HOG ϸҴSĸȯ4ҍ`dgG;OceՕr´·ȺϓȾjέҍ?G%
Ņ1MՕAnNikA SѤű HK RK/Maų˭R HK ˶ЫΜѰȾOr´·ȺϓȾjέҍ?Օ̴ӋƝĹ͔SɊŧRӳѵO=gf HAMP ©o·S˶Ы4Ѥű AnNikA RЂɪ=gM/f;Ojέҍ?G%ͲƞՕįцӮ̋R
2/M HK ˶ЫΜѰȾjέҍ?GѤű HK RK/MϩͪёNSΑͲϪjˬϚ?ՕѾˊjӑ`M/f%(ˀΧσTՕ͹Χ ·¹o¡¹¯·ŁįƨήΕΧσɷӑÐ˩OӀˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩Sʆɼjŧ9MѦigGaSN.f%)
Functional complementation and ethylene response of plant-fungal fusion histidine kinase in budding yeast andfilamentous fungi.
Mayumi Nakayama1,2, Kentaro Furukawa3, Akira Yoshimi1, Keietsu Abe1,2(1NICHe., Tohoku Univ., 2Grad. Sch. Agric. Sci., Tohoku, Univ., 3 Univ. of Gothenburg)

O-8 (P-64)
Functional binding characteristics of ManR/ClrB to regulate cellulase and mannanaseproduction in Aspergillus nidulans
Nuo Li, Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi(Grad. Sch. Bioagric. Sci., Nagoya Univ.)
 ManR in Aspergillus oryzae and ClrB in A. nidulans, which are orthologous to each other, were identified
independently as transcriptional activators involved in mannanase and cellulase genes. Cellulase genes are under control
of not only ManR/ClrB but also McmA that contributes to activation of cellulase genes via recruiting ManR/ClrB to
CeRE (Cellulose Responsive Element). In the case of mannanase genes, McmA is generally not required. It has beenshown that ManR binds to the promoter region of mndB that encodes β-mannosidase without assistance of McmA.
To identify the functional binding site for ManR in vivo, DNA fragments of three binding sites (CGGN8CCG) on the
mndB promoter were independently fused to the coding region of A. oryzae α-amylase gene (taaG2) and integrated at
the argB locus of A. nidulans genome. The transformants that exhibited highest amylase activity in response to cellulose
carried the sequence CGGAGCGAAACCCG that located at -547 ~ -560 relative to the translation start site of mndB,
which indicated that this region works as the recognition site of ManR in vivo. Meanwhile, the recognition sequence of
ManR on the promoter of the endoglucanase gene eglB was examined in vitro by supershift assay. The ManR-McmAbinding site of eglB consists of two overlapped CeRE in the opposite direction (CCGN2CCN6GGN2CGG). Mutation of
CCG and CGG led to stronger binding of McmA and loss of McmA assisted ManR binding. This implies that ManR
binding to CeRE is supported by interaction with McmA as well as the CGG triplet. All above discoveries will help tounderstand the binding property of ManR that involved in regulatory function.
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.

 29 —O-9 (P-62)
ՊёSҸĩƔǇ FlbC TƙóƧԸͨ·ΕΑͲjίAz³}m§±¹ӟêǇՒglaBՓSΑͲjĸȯAf
Ų˄ЇՕͼÂͷȃՕʗҝǫȜՕÓż ŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓՊёSƙóƧԸͨ·ΕR͹ͺ=gfz³}m§±¹ GlaB TՕёϩɐԁԉǘ˅åՕï̒İ̭Ⱦ˅åՕԿ̈́ƧԸ˅åO/0 3 ˅åRce´¹ƧԸNaҎǨ͹ͺ4ūЫN.f%;S˅åj͇GAƧԸ˅åO?MՕ
50%¦³¹jŶ_ǟƻƧƠՒï̒İ̭ȾՓRһCGoµ·г¼ՒёϩɐԁԉǘՓNՊёjƧԸ?Օ
oµ·гRİ̤ŷΠ=gG GlaB jɝóŤȺNĨͲȾԿ7˧įAf;ORɐń?G%;Sʘ̥jͻ/MҸĩƔ
ǇΩƳ˗±o±²¹434 ˗Sy²¹·zjѦ/ՕӞɞ?G 19 ˗RK/MǩՈXA]jͻ/GƙóƧԸjѦ/Օz³}m§±¹̭ȾO α-m§±¹̭ȾjͅǓ?G%ESϹˌՕα-m§±¹̭ȾRǣAfz³}m§±¹̭Ⱦ4 glaB ΩƳ˗Oųνȑ]Nï½?G˗4 1 ˗ȮdgG%;S˗Tİ͹ǇȢɐRԅif;O4Ƭź=gM/f C2H2 ƣҸĩƔǇ FlbC SӟêǇΩƳ˗N.JG;O3dՕFlbC Oų˭SϸҴN˶ЫAfßSҸĩƔǇΩƳ˗RK/M GlaB ͹ͺjғZG4ՕԱјQ͹ͺï½Tҍ`dgQ3JG%=dRՕGlaB Oų˭RƙóƧԸNͨ·ΕR͹ͺ=gfµm¹Oµ¹jͅǓ?GO;hՕflbC ΩƳ˗NTӯȾµm¹̭ȾSï½4^dgՕFlbC T GlaB SΑͲH9NQ7ӯȾµm¹ӟêǇSΑͲRaԅ¿A
fūЫȾ4ίƅ=gG%
ՒˀΧσT'Ӏˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%Փ

The Aspergillus oryzae transcription factor FlbC involved in the expression of the glaB gene specifically
expressed in solid-state culture
Midori Yoshimura, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi
(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric., Tohoku Univ.)O-10 (P-74)
Aspergillus aculeatus R29f dipeptidyl peptidase 4 S˶ЫѾˊӓÍИƼՕƛ˾ϾЕՕҝĆ̠Օ͙ҝԬºՕǿũĽů ՒԇȐƺԍ¸͹͸θՓɑ&TՕA. aculeatus T-DNA ɰĢƷ·˗±o±²¹3dŘԝ?G ³µ¹ҎǨЫ˸ɽ˗R2/MՕ
dipeptidyl peptidase 4 (dpp4) ӟêǇ4ΩƳ=gM/f;Ojѷ/H?G%A. aculeatus DPP4 T A. fumigatus šWƄÌԲS DPP4 OEgFg 67 %Օ31 %SΜųȾjʸ?M2eՕDPP4 T͹ͧR2/MȎ7Ąǉ=gM/fӮ
ϰN.f%ƄÌԲ DPP4 TՕ¢£³ª·S N ʿϊĐ3d 2 ΆΚS Pro ]GT Ala S C ʿϊĐjıʕA
f;ON˭&Qz³êӘjĸȯ?M/f%Aspergillus RTՕdpp ӟêǇ4 4 οǉƞAf4/BgSӮϰa͹ʹ˶ЫRԅAfƬźTQ/%E;Nɑ&TՕϩͪёR29f DPP4 S˶ЫjѾʣAf;OjΚΕO?MΧ
σjӑ`M/f%ʗGRöį?G dpp4 ΩƳ˗ (Δdpp4) R2/M cellobiohydrolase I ӟêǇϑSm ³b µt¹RceҎǨ=gfӟêǇSΑͲTՕҎǨĳʼRԌǓΕŔǪ?M/G%ºʘՕxylanase Ib ӟêǇϑSw±·bwµ¹RceҎǨ=gfӟêǇSΑͲӵTƷŎ?M/Q3JG;O3dՕDPP4 T ³µ¹ҎǨSĸȯRԅ¿?M/f;O4ί=gG%˹R}·µ¹³˗ՕΔdpp4Օdpp4 ԿΑͲ˗ (dpp4-OE) R29f DPP ̭Ⱦ
j Gly-Pro-pNA jƨҮRͻ/MͅǓ?GϹˌՕdpp4-OE R2/MʸɈR DPP ̭Ⱦ4¼ʢ?M/G%]GՕΔdpp4NT}·µ¹³˗O̎Һ?MёóΩΨȫSū͋Ⱦ΁İS̭ȾRTƺ5Qә/4Q3JG4Օёó̄̓S
Triton X-100 ū͋Ŏ΁İNTϬ 2/3 Rï½?M/f;O4ҍ`dgG%;S;O3dՕDPP4 4гRϹű?M/f;O4ɷͅ=gGG`ՕͲƞ DPP4 SǯƞѾˊjѦJM/f%]GՕΔdpp4Օdpp4-OE R29fȢҮSƷŎaͲƞѾˊÂN.f%
Functional analysis of dipeptidyl peptidase 4 in Aspergillus aculeatus
Syota Yuki, Emi Kunitake, Shuji Tani, Jun-ichi Sumitani, Takashi Kawaguchi(Grad. Sch. Life & Env. Sci., Osaka Pref. Univ.) 30 —O-11 (P-37)
Maintenance of active directional growth by perpetual assembly and disassembly of polarity
sites
Norio Takeshita1,4 Yuji Ishitsuka2, Natasha Savage3, Yiming Li2, Anna Bergs1, Daria Kohler2, Rebecca Donnelly3, G.
Ulrich Nienhaus2, Reinhard Fischer1Ւ1Dept. of Microbiology, Inst. for Applied Bioscience, 2Inst. for Applied Physics,
Karlsruhe Institute of Technology (KIT). 3Dept. of Functional and Comparative Genomics, Inst. of Integrative Biology,
Univ. of Liverpool. 4Univ. of Tsukuba, Faculty of Life and Environmental Sciences.)
Polar cell extension depends on spatially very defined insertion of new membrane. In filamentous fungi, like
Aspergillus nidulans hyphal tips (3 µm in diameter) extend with speeds of 0.3 – 1.0 µm per min, which means anincrease of the membrane surface of 0.9π – 3π µm2 per min. Given that secretory vesicles are about 40 nm in diameter,
massive exocytosis of about 600 – 2000 vesicles per min is required to ensure sufficient membrane supply even in thecase that endocytosis is ignored. On the other hand, secretion at the hyphal tip depends on the exact positioning of
landmark or cell-end marker proteins, anchored in the membrane. The active exocytosis in filamentous fungi has apotential to diffuse membrane associated polarity markers but they can maintain the polarity to form hyphae. Here, we
discovered a mechanism how polar growth can be maintained despite the continuous, massive disturbance of cell-end
marker positioning caused by membrane insertion. In A. nidulans the cell-end marker protein TeaR reaches the tip
through microtubule- and actin-dependent transport. Once at the tip, TeaR recruits other proteins among which is theactin forming formin SepA. Thus the actin cytoskeleton assembles at the site of TeaR, and delivers more TeaR to thissite. This positive feedback loop causes increased secretion, local membrane extension, but also dilution of the cell-end
markers. To solve the contradiction, the polarity is reconstructed by microtubules repeatedly in addition the cell growth,
membrane extension, occurs in a fluctuation manner. The localization and dynamic behavior of TeaR is investigated bysuper-resolution microscopy technique PALM (photoactivation localization microscopy).

O-12 (P-38)
İ̤Ӯϰ͹ͺRԅ¿Af Aspergillus nidulans SunA S˶ЫѾˊпǵ.B^ՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ¸͹žӀǋՓ)ΚΕ* AHP1102 Tm§±¹Օ ³±¹Օµm¹QPİ̤ӮϰS͹ͺȾ4ŵ¼?GƷ·˗N.e sunA ӟêǇTˀƷ·jΜѰAf%A. fumigatus R2/M SunA St³µz Sun1 TϳЩƲ β-1, 3-glucan
RöͻAfӮϰN.f;O4ӄȌί=gM/f%ˀΧσNT SunA S˶ЫՕE?Mİ̤Ӯϰ͹ͺȾR¿1f
ȦԪjѾˊ?G%)ʘ̥¸Ϲˌ* ]B AHP1102 R29f sunA ӟêǇ¼SƷ·jųǓ?G%ESϹˌՕ;SƷ·Tyµª
¹¨ I S sunA Sµª¹¹ԮƦOyµª¹¨ VIII S AN0430 ˬӏӟêǇħOSϷ^ɺ1Rce͹@G;O4ʣd3OQJG%SunA 4İ̤Ӯϰ͹ͺȾRȦԪj¿1f;OjέҍAfG`ՕΩƳ˗ՕԿΑͲ˗jöѱ?G%ΩƳ˗NT AHP1102 Oų˭Rİ̤ӮϰS͹ͺȾŵ¼4^dgG4ՕԿΑͲ˗NTʸɈQȦԪTѷdgQ3JG%]GՕёóƸ·yҮj SDS-PAGE N̎ҺAfOՕΩƳ˗NTӴȾ˗R̎Zƹ˭Q·yҮ4ёóƸRǉƞAf;O4ʣd3OQJG%SunA 4ϳЩȢɋR¿1fȦԪjԱȲӿѼǡ?GO;hՕΩƳ˗NTёϩSȢͪ4/WKRQfQPS·ȉ4^dgG%ʳRTϳЩƲRöͻAfŎǋͧҮN.f
Calucofluor white, Congo red QPRǣAfΩƳ˗SɊŧȾjӴȾ˗O̎Һ?GO;hՕΩƳ˗NTɊŧȾjί
?G%;gdS;O3d SunA SϳЩƲűɐ¸İѾYSԅ¿4ίƅ=gG%ºʘNϳЩƲSȿȉȾRԅ¿A
fҸĩƔǇՕɆƬêӘƔǇO sunA ӟêǇΑͲOSԅāj˧҂?G4ՕnikA, mpkA, rlmA /BgSΩƳa sunASΑͲRȦԪj¿1Q3JG%Functional analysis of Aspergillus nidulans SunA involved in extracellular enzymes production
Azumi Funayama, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi(Graduate Sch. of Bioagric. Sci., Nagoya Univ.) 31 —O-13(P-40)
ϩͪё§}·²mS˶ЫYS·w¹ HysA Sԅ¿ˋʟϫՕǩǺɏÝՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽՒŴƺԍ¸͹žӀՓϩͪёS͸ưȺϓRTՕ͹ͧRȎ7Ąǉ=gG His-Asp ²·ӯ²´¹ɆƬêӘ˶ˬ4ӳѵQȧŀjɣJM/f;O4΢dgM/f%;S¨NTՕ͸ư ·¹N.f·w¹ՒHKՓ3dS²·ӯƨҸλRcJMɆƬ4ϳЩħRêӘ=gf%âļigigTՕª³ϩͪё Aspergillus nidulans S HK ΩƳ˗Ւ13 οԲՓR29f̭ȾӯϰοՒROSՓSΑ͹jѼǡ?ՕHysA SΩƳ˗R2/M ROS SΑ͹´¡³4Կ
/;Ojѷ/H?G%ӯϰŽŷjѦ0͹ͧNTՕ§}·²mSԠǇêӘϪN ROS 4Α͹Af;O4΢dgM/f%§}·
²m4˽ȉQԕRT ROS j̍͜ŎAf;O4ūЫH4Օ§}·²m4˶Ыjƿ0OΑ͹?G ROS 4ϳЩħRњς?Օ·yҮb DNA R©¹j¿1f%hysA ΩƳ˗R2/MΑ͹?G ROS TՕ§}·
²m˶ЫSƷŎRcJMΑ͹њς?GūЫȾ4Л1dgG%E;NՕhysA ΩƳ˗j 3 ʜԄƧԸ?ՕгԠîS͹@G̭ȾŎ§}·²mj˧įAfѣĞсϰՕMito Tracker Red Nˑс?ՕԱȲӿ½NѼǡ?G%ESϹˌՕΩƳ˗NTՕ̭ȾŎ§}·²m4İ͹ǇːR2/MčJMǯƞ?M/G%ROS SΑ͹Tİ͹Ǉː
R2/MʶaȠ7Ѽǡ=gf;O3dՕ;Sče4 ROS Α͹SŞƔN.f;O4Л1dgG%ˀΧσNTՕЇсѣĞ·yҮ GFP jͻ/G HysA SǯƞѾˊSϹˌaøCՕɆƬêӘƔǇN.f HysA 4PSc0R
ϩͪё§}·²mS˶ЫRԅ¿Af3ЛǡAf%
Possible involvement of Histidine kinase HysA in mitochondrial function of Aspergillus nidulans
Saki Hayashi, Kensuke Kojima, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi(Graduate Sch. of Bioagric. Sci., Nagoya univ. )O-14 (P-32)
Պё A. oryzae R29fĞýǉȾSİ͹ǇȢɐɛĸ©u¨RԅAfѾˊ
Helge M. DietrichՕͼÂŉ̑ՕӶ ӹˇՕÃǵ͒ºՕŏˀŌV;Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓՊё Aspergillus oryzae R29fİ͹ǇȢɐTՕοՊӏebё˗S˦ё¸ĄǉQPSͺ˩ΕĶͻRȦԪAf
ӳѵQӖνN.f%ɑ&TâļՕĞRcJM A. oryzae Sİ͹ǇȢɐ4ɛĸ=gf;OjƬź?G 1)%ºʘNՕ
Aspergillus nidulans QPNƬź=gM/fc0RՕĞ4´OQJMİ͹ǇȢɐ4Ăӑ=gfS4ºоΕ
N.fOЛ1dgf4ՕA. oryzae SȺϓT;gOT˽ŤǣN.f%A. oryzae 4Ǚ΅Ŏ=gfԕRՕʲ/ǱħSοՊӏeNİ͹Ǉjƹ7ȢɐAf˗4Ӟɟ=gM5GūЫȾ4Л1dgf4ՕESİǇ©u¨T¾ʣ
N.JG%ÜƓTՕ͠ǤAfĞŞԁjӞɟN5f LED Ğ͈jùͻAf;ORceՕA. oryzae 4ĞRȺϓ?
Mİ͹ǇȢɐjɛĸAf©u¨Rԅ?MѾˊjѦJG%ԢсĞ2cWүсĞ͠Ǥ˅åN A. oryzae RIB40 ˗SƧԸjѦ/Օİ͹ǇSȢɐňͯRK/MғZG%ESϹˌՕԢсĞ͠ǤRcfİ͹ǇȢɐSɛĸ4ѷdgG4ՕүсĞNTĞSȦԪTѼǡ=gQ3JG%;S;O3dՕĞRcfİ͹ǇȢɐSɛĸTԢсĞRýǉAf;O4ί=gG%;SĞȺϓS©u¨jѾˊA
fG`ՕA. oryzae |¨¹¡¹ceՕA. nidulans SԢсĞŧǚó LreA OүсĞŧǚó FphA RΜųQ·yҮj}¹AfӟêǇjѷ/H?ՕEgFg AolreAՕAofphA OžŴ?G%ӟêǇΩƳ˗jöѱ?GϹˌՕAolreA ΩƳ˗R2/MԢсĞRcfİ͹ǇȢɐSɛĸ4ѷdgQ7QJG%ºʘNՕAofphA ΩƳ˗NTՕӴ͹ƣ˗Oų˭RԢсĞRceİ͹ǇȢɐ4ɛĸ=gG%?G4JMՕA. nidulans S LreA O FphA TĞ
RȺϓ?ՕŖғ?Mİ͹ǇȢɐjĂӑAfSRǣ? 2)ՕA. oryzae NT AoLreA S^4ĞýǉΕRİ͹ǇȢɐjɛĸ?ՕAoFphA T;SӖνRԅ¿?Q/;O4ʣd3RQJG%
1) Hatakeyama et al. (2007) Biosci. Biotechnol. Biochem. 71:1844-9. 2) Purschwitz et al. (2008) Curr. Biol. 18:255-9.
Investigation of light-dependent repression of conidiation in Aspergillus oryzae
Helge M. DIETRICH, Yuki TANAKA, Feng Jie JIN, Jun-ichi MARUYAMA, Katsuhiko KITAMOTO(Dept. of Biotechnol., Univ. of Tokyo) 32 —O-15 (P-33)
u¹¤·u¤±oɛĸĸȯƔǇ CreA ṰȾŎ˅åR2/MǍǓŎAf
ͼÂͷȃՕʗҝǫȜՕÓżŌËՒˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓ ϩͪёSu¹¤·u¤±oɛĸT, C2H2 ƣҸĩƔǇ CreA RcJMĸȯ=gf;O4΢dgM/f%
Aspergillus nidulans NT, u¹¤·u¤±oɛĸRԅifßSƔǇO?M®w·ŎbЯ®w·ŎRԅ¿AfƔǇ4ųǓ=gM2e, ;gd4 CreA SİѾRԅ¿AfūЫȾ4ɫʀ=gM/f%?3?,
CreA SǍǓȾRK/MT[OkP΢ѷ4Q/%ˀΧσNT, m§·̼ŅRceΑͲɛĸūЫQ thiA µª¹¹ĸȯ½N 3FLAG zѤű CreA jՊёNΑͲ=C, ˭&Q͙ϰ͈ǉƞ½R29f CreA SǍǓȾjѾˊ?G% ļƧԸ?G 3FLAG zѤű CreA ΑͲ˗Sёójm§·̼ŅƧƠRλ?MΑͲjɛĸ=CGȫ, Űο͙ϰ͈j̼Ņ?, ϸʪΕR CreA ·yҮӵjғZG%ESϹˌ, ͙ϰ͈jŅ1Q/ƭűb¦³¹, ³y¹, wµ¹, z² µ¹³j̼Ņ?GƭűRT CreA TȽӎRİѾ=gG%ºʘ, z³}¹b¦·¹j̼Ņ?GƭűRT CreA 4ј?7ǍǓŎ?G%Űο͙ϰ͈Su¹¤·u¤±oɛĸYSԅ¿jғZfG`, ··ƧƠRŰο͙ϰ͈j̻ű?, µ¹ȢɐЫj̎Һ?G%ESϹˌ, z³}¹O¦·¹j̼Ņ?GƭűRӴ͹˗Sµ¹ȢɐЫ4 creA ΩƳ˗O̎Һ?Mј?7ɛĸ=gG%â¼SϹˌ3d, CreA Tu¹¤·u¤±oҎǨ˅åR2/MǍǓŎ=gf;O4ίƅ=gG%Ͳƞ, CreA SϳЩħǯƞb®w·¸Я®w·ŎԅӐƔǇS CreA ǍǓȾYSԅ¿RK/MѾˊjѦJM/f%ˀΧσT'Ӏˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%
Stabilization of carbon catabolite repression regulator CreA under the activation condition in Aspergillus oryzae.
Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi
(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ.)O-16 (P-83)©µ³¢o anditomin ͹űɐSģǚѾʣˉͼûƺՕ̸ǿǊЗՕЭˀʋȍՕԊӧӥʺ Ւˈƺԍ¸џՓ©µ³¢oOTՕ³¢oSӧİˬӏjʸAfŎűͧSІκN.eՕϩͪё3dTˬӏƹ˭Ⱦ
QdWR͹̭ͧȾRǞ_ƹʎS©µ³¢o4Ƭź=gM/f%Aspergillus variecolor Sͺ͹Afanditomin TՕͨ·QİǇħˏ˵ˬӏjʸ?M2eՕES͹űɐSİǇƨΙRкż4ɪGgf%ɑ&TՕʨȌȑSˀéRM anditomin ͹űɐӟêǇy±¹SųǓjƬź?G%;g]NRՕ͹űɐĳʼ̆ԓjɣ0 5 K
SӮϰS˶ЫѾˊjѦ/ՕÓ͸ȾSİǇԾ˚jʸAf͹űɐÂԄóՒŎűͧ 1ՓSŘԝRɐń?M/f%Ü
ƓʗGRՕˀӟêǇy±¹S}¹Af 7 KSĆԷӮϰS˶ЫѾˊjѦ/Օanditomin ͹űɐSİǇƨΙѾʣjΚɫ?G%Ŏűͧ 1 âԋS͹űɐϸҴjÏͅAf;OTƖԞN.JGG`Օ·οϩͪё Aspergillus oryzae RMο&SϷ^űiCSĆԷӮϰΑͲϪjˬϚ?ՕȮdgGȢҮҸɺóR 1 jɜ¿ȫՕESáҚͧjİˊAf;ONՕŰĆԷӮϰS˶ЫQdWR͹űɐϸҴjɷǓ?G%Ű͹űɐÂԄóSŘԝՕˬӏ̙ǓR.GJMTՕŎűͧ
1 SűɐRԅif 5 KSӟêǇaűiCMΑͲAfϪjԬ˹ˬϚ?G%Ņ1MՕºӧӮϰRK/MTƺбёRMƺӵΑͲՕϦѱȫ in vitro S҉ԽRü?G%â¼RceՕanditomin Sģ͹űɐϸҴSѾʣRɐń?G%ˀ͹űɐR2/MTՕFe(II)2cW α-{z³³ӯýǉƣtw|¹ AndA 4Ñ̆ԓSŤȺjѿǆ?Օ
ͨ·Q bicyclo[2.2.2]octane Ծ˚Ȣɐjɣ0;O4Ĵʣ?G%]GՕ͹űɐSʶ϶̆ԓNTՕbTetw|¹N.f AndF 4ӯŎΕҸîŤȺRce anditomin SİǇԾ˚j¿1f;Ojѷį?G%
Complete biosynthetic pathway of fungal meroterpenoid anditomin
Yudai Matsuda, Takayoshi Awakawa, Toshiyuki Wakimoto, Ikuro Abe(Graduate School of Pharmaceutical Sciences, Univ. of Tokyo) 33 —O-17 (P-86)
ϩͪё Aspergillus nidulans RcfƜƴ§·ӯSˬӏƷŎÂ͓ǀЕՕК̡ΧºՕԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓƜƴRҟǞRŶ]gf§·ӯT, ˦ͧ²z·ϑRͽˆAfхԺ͸bЬФʚӾjƹ7Ŷ_ԞİѾȾSԿ
İǇŎűͧN.eՕз͞΂NT͹ͧΕ]GTԥ͹ͧΕRİѾ=gf;ORcJMƠͳ¼S͙ϰȱ͸SЂɪRҢͬ?M/f%?3?Q4dՕºӧSϳёbΓсаˁёjԎ/GёԲO§·ӯOSΜÒöͻRK/MT[
OkPʾѾʣN.f%ˀΧσǖNTՕ;g]NRՕ Aspergillus nidulans S DNA ¦oyµm´oѾˊ3dՕ§·ӯS̼ŅRcJMˀёSѲʎSӯŎӮϰӟêǇSΑͲ4¼ʢAf;Ojѷį?M5GՒ2013 ȑՕˀ}·l´·Αѫ P-22Փ%
E;NՕˀΧσNTՕ A. nidulans SƧԸRë0§·ӯSˬӏƷŎSѾˊj҉^G%A. nidulans TƧԸR
ëJMƧƠÂS§·ӯjŷΠ?G%ёRŷΠ?G§·ӯOƧԸ̶ÂS§·ӯjEgFgƓť?Օ¹²rƷɺƣүƸİĞѾˊՒFTIRՓjѦJGO;hՕPIdaЬФʚՕm²³r¹³Օq¹³SƱŅ4
Ѽǡ=gG%ƧԸȫSƧԸ̶ÂS§·ӯSƙó 13C NMR ceՕu³¤wƨO©wƨSƱŅ4ՕԠîȂ͏ǓRcfǑЫƨİˊceՕu³¤·ӯOq¹³SŶӵ4ƱŅAf;O4ί=gG%]GՕ|³hӖİˊRceՕƧԸRëJM§·ӯ4ԿİǇŎAf;O4ʣd3OQJG%â¼S;O3dՕ§·ӯTΑͲҎǨ=gG A. nidulans SӯŎӮϰЖSė5RcJMӯŎӳű=gM/fOЛ1dgG%§·ӯS̼ŅRcJMԱјRҎǨ=gf Flavin-containing monooxygenase (AN10582)SӟêǇΩƳ˗jöѱ?MƧԸȫS§·ӯS FTIR ѾˊjѦJG4ՕǑЫƨSƷŎTӴ͹ƣ˗OƷidQ3JG%ͲƞՕ§·ӯSӯŎRԅifӟêǇSͨǓj҉^M/f%
Structural changes of soil humic acid by the fungus Aspergillus nidulans
Nami Nakazawa, Ken-Ichi Oinuma, Naoki Takaya(Faculty of Life and Environmental Sciences, Univ. of Tsukuba)

O-18 (P-92)
Ŏűͧm´ojͻ/G©±·͹űɐԉǘľɵϱˀǵԿȍ 1,2ՕͼÂԑǇ 2ՕԁͼѯÇ 1,2Ւ1 ʹΧ¸ɝ͹ͧҮՕ2 ʹΧ¸CSRSՓ
【目的】イネいもち病菌の二次代謝産物メラニンは病原性に必須であるが生育には必要とされないため，生合成系の酵素は環境負荷が低い農薬の標的として注目されてきた。メラニン生合成系の 2 種類の標的酵素（3HNR，Sdh1）に対する農薬（MBI-R，MBI-D）が開発されてきたが，既存の農薬は耐性菌などの問題を抱えており，新たな制御薬剤の開発が求められている。我々は，天然化合物バンク NPDepo を設立し，標的タンパク質に対する結合化合物探索を超ハイスループットで行うことが可能な化合物アレイを開発してきた。
今回，化合物アレイを用いた NPDepo 化合物からのメラニン生合成阻害剤探索について報告する。
【方法と結果】メラニン生合成系の標的酵素として，非還元型ポリケタイド合成酵素（NR-PKS）Alb1，ヒド
ロキシナフタレン還元酵素 3HNR，シタロン脱水酵素 Sdh1 を選択した。Sdh1 については，野生型酵素 Sdh1-WTと農薬耐性型酵素 Sdh1-V75M を用いた。それぞれの標的酵素を大腸菌で発現・精製し，化合物アレイスクリー
ニングを行った。NPDepo の約 3 万化合物の中から，Alb1，3HNR，Sdh1-WT，Sdh1-V75M に対してそれぞれ，
21 個，21 個，4 個，8 個のヒット化合物を得た。3HNR のヒット化合物の阻害活性を解析したところ，1 化合物（リファマイシン誘導体）が阻害活性を示した（IC50=25 µM）。従来のスクリーニング法と化合物アレイによるスクリーニング法との違いについて報告する。
本研究の一部は，農林水産業・食品産業科学技術研究推進事業による支援を受けた。
Chemical array screening of melanin biosynthesis inhibitors
Takayuki Motoyama1,2, Yoko Tanaka2, Hiroyuki Osada1,2(1Antibiotics Lab, RIKEN, 2CSRS, RIKEN) 34 —O-19 (P-94)
p²Բ͙ΌΎёR29fįцӮ̋´ȺϓĸȯƔǇ WHI2 S£ªµz CoWHI2TǛÄԈȯȺϓSҎǨO͉̭ͧǜ͹ȾSĸȯRԅ¿AfŞͼ Ҭ, ÆĄȔÇ (ÙȐƺԍ¸͹͸)ʨȌȑSˀéRM,p²Բ͙ΌΎёS CoRas2 TɊˑƏǑSȢɐӖνRo§yQǯƞjίA;OjƬ
ź?G%įцӮ̋S Whisky2(Whi2)T Ras SϳЩħǯƞSĸȯbsl¹j}¹Af Psr1 OϹűAf;ORceҸĩƔǇ Msn2 jЯ²·ӯŎ?, STRE(Stress response element)jʸAf´ҎǨӟêǇSΑͲjĸȯAf;O4Ƭź=gM/f%E;N,Ras SʪτԄΕQĸȯOɊˑƏǑSȢɋȢɐSԅāRK/M
ғZfG`R,ɑ&Tp²Բ͙ΌΎёR29f WHI2 S£ªµz CoWHI2 RΠΚ?,˶ЫѾˊjѦJG%]
B,CoWHI2 4ΎŞȾbɊˑƏǑSȢɋȢɐRԅ¿AfS3,cowhi2 ˗jöį?,˧҂?G%ESϹˌ,cowhi2
˗Sw­p²RǣAfΎŞȾTӴ͹˗O̎Һ?,ï½?G% ]G,cowhi2 ˗SÿĢёϩTӴ͹˗O̎Һ?,́ͧǜ͹Ⱦ˭Sϳ/Ȣɋjί?G%кż̹/;OR,cowhi2 ˗TӴ͹˗O̎Һ?,ǛÄ˦ͧSuµ¹ȢɐjԱјRҎǨ?G%E;N,cowhi2 ˗Tuµ¹ȢɐRԅifuµ¹űɐӮϰӟêǇSΑͲjҎǨAfS3,
cowhi2 ˗ɶοїSuµ¹űɐӮϰӟêǇSΑͲӵj qRT-PCR jͻ/,ϸʪΕRͅǓ?G%ESϹˌ,
cowhi2 ˗ɶοїNTӴ͹˗ɶοїO̎Һ?,ʟʼRµo ATGSL4,ATGSL8 S£ªµzSΑͲӵ4Ʊ
Ņ?G%;S;O3d,CoWHI2 Rcfuµ¹ȢɐSҎǨT;gdSuµ¹űɐӮϰӟêǇRұƔAfūЫȾ4ίƅ=gG%˹Rcowhi2 ˗T́ͧǜ͹˭ÿĢёϩjȢɐ?G;O3d,́ͧǜ͹ёRǣ?ΑͲ4ƱŅ
AfµoS PDF1.2 Sw­p²R29f£ªµz DEFENSIN19 SΑͲӵj qRT-PCR jͻ/,˧҂?
G%ESϹˌ,cowhi2 ˗ɶοїS DEFENSIN19 SΑͲӵTӴ͹˗ɶοїO̎Һ?,ԱјRƱŅ?G%â¼3d,CoWHI2 TǛÄԈȯȺϓSҎǨO͉̭ͧǜ͹ȾSĸȯRԅ¿Af;O4ίƅ=gG%
CoWHI2, the homolog of stress response regulator WHI2 of Saccharomyces cerevisiae, is involved in induction ofhost defense response and regulation of hemibiotrophic infection in Colletotrichum orbiculare.
Ken Harata Yasuyuki Kubo (Life and Environmental Sciences, Kyoto Prefectual Univ.)

O-20 (P-104)¦o}po³ɊˑRcfϩͪёϳЩƲSˬӏƷŎʻʷИǇՕӷʽąȜՕύŞϴ ՒǗƥƺ¸Գͺ˩¸͸ưՕǷǵƺ¸˦ͧΧՓϩͪё Cryphonectria parasiticaՒʝ Endothia parasiticaՓTĭÌ̭ȾjίAӯȾµm¹jԿͺ͹?Օ
i4ƚNaŪ73dΧσǣҠO=gM5GϩͪёN.f4Օy²QPSˌ˴Rǣ?MЪˎΎjț5ұ;A˦ͧΎŞёNa.f%100 ȌõeļRʜˀ3dϟƚˈӧRaGd=gGˀё4ՕɊŧȾSԿ/m©²uz²
ՒAmerican chestnutՓjǵӴ3d[\ºɴ?G;OT˦ͧΎʹǋŭ¼ՕͨRʸŴN.f%C. parasitica Tpo³Ւ¦o}po³ՓɊˑRceёϩɐԁӎȑbЩǇȢɐЫ4ï½?ՕΎŞȾa[\̵ƿAf;O4΢dgM/f%]GՕpo³ɊˑRceϳЩƲ͋ѾӮϰYSɊŧȾ4ƱƺAfQPՕϳЩƲSˬӏ4ȦԪjŧ
9M/fOSÏĒΕ΢ѷ4.eՕԥpo³Ɋˑ˗Opo³Ɋˑ˗SEgFgSϳЩƲRΠΚ?MϳЩƲˬɐƹϧSİ΁OǓӵՕˬɐϧİˊϑjѦJG%w·ϹűȾSѣĞсϰ Calcofluor White Rcf C. parasitacaϳЩƲÂw·SǯƞѼǡNTՕԥpo³Ɋˑ˗N.f EP155 ˗Օpo³Ɋˑ˗N.f EP713 ˗Օ
CHV2/EP155 ˗ՕMyRV1/EP155 ˗NEgFgѣĞȠȑ4ƷŎ?M/G%ϳЩƲƹϧSİ΁ǕԽNTՕԥpo³Ɋˑ˗Opo³Ɋˑ˗ԄNՕw·jŶ_ AI ΁İSҮӵRʸɈȂTѷdgQ3JG4Օα13z³u·jŶ_O=gf AS2 ΁İR2/MTՕpo³Ɋˑ˗Sƹ7NҮӵ4́Ǫ?M/G%]GՕˬɐϧİˊSϹˌceՕԥpo³Ɋˑ˗Opo³Ɋˑ˗NTՕϳЩƲƹϧjˬɐAfŰŘϧɐİS̎ͯRƺ5Qә/TѷdgQ3JG%;gdSϹˌceՕpo³ɊˑRceϳЩƲÂSα13z³u·ӵ4ʸɈŔǪ?Օ
;S;O4ΎŞȾOԅӐ?M/fūЫȾ4ίƅ=gG%

Structural changes in fungal cell wall caused by mycovirus infection.
Shoko Mochizuki, Nobuhiro Suzuki* & Shin Kasahara(Miyagi Univ. School of Food, Agric. & Envron. Sci., *IPSR, Okayama Univ.) 35 —







Poster Session
P-1
̦ΗӱӏRͻ/dgM/fՍՊёSϪϽǋΕѾˊƮŞ˽ă 1Օ͂ÆƠʊ̘ 1Օȩ̀ʹƁ 1Օˈʧǀ 1ՕƺƥȤԩ 1Օ͂Ӣ̩α 2ՕƸǵřщ 2ՕǵͼĆ 3Ւ1 otqՕ2 ͵ͳƺӀ¸Õ͢͹ҪՕ3 ӫІΧՓ ̛ЍΞSêϽӫ'̦Η(T 600 ȌS̀ŭjʸAfʜˀʶŪSљ΄ӫN.f%ͲƞՕƇ˩Ε̦ΗӱӏRTՕՍՊёO?MՕm¶ª²ёՕooёՒģMSӫӏɕRMՙο̻űĶͻՓՕ2cWɒļ3dSĄǉё˗jȰĺ?Gͷ̣ёՒͷ̣ӫӏՓ4ͻ/dgM2eՕ;gdTǍģ3KęgGӱӏͨȾjʸ?M/f;O4έҍ=
gM/f%;gdSՕ̦ΗՍՊёTԁ/Ԅ Aspergillus awamori RİԲ=gM5G%?3?Q4dՕ A.awamori
2cW A.niger RTՕˀˆSİԲ=gfZ5ƹʎS˗4ΜÒR̻ƞ?M/fƈ԰͚4ɫʀ¸˧҂=gGϹˌՕ
A.luchuensis O/0ǋŴ4ҍ`dgfOĥRՕA.luchuensisՕA. tubingensisՕA. niger S՚οRĨʏʹ=gGՒǵͼdՓ%ÜƓՕѲʎё˗Sģ|¨ѾˊjѦ/Օ̦ΗӱӏRͻ/dgfՍՊёSҋϳQϪϽѾˊjѦJG%E
SϹˌՕm¶ª²ё2cWͷ̣ёTʛƬSӍe A.luchuensis N.f;O4ί=gG%ºʘՕ˰͉˗O=gM/
f A.saitoi NRRL4757T T A. tubingensis RİԲ=gfOƬź=gM/f%?3?Q4dՕ̦ΗӱӏRͻ/dg
M/fooёTՕm¶ª²ё2cWͷ̣ёOų@ A.luchuensis N.f;O4ʣd3OQJG%Classification of black koji molds for Awamori brewing
Masatoshi Tsukahara1, Shota Toguchi1, Tomoya Iha1, Haruna Azuma1, Ayane Oshiro1, Taisuke Watanabe2, Hirohide
Toyama2, Osamu Yamada3 (1Biojet, 2Univ.Ryukyu, 3 NRIB)

P-2
Influence of light on growth and conidiation of Aspergillus oryzae
Pushpa S Murthy1, 2, Ken-Ichi Kusumoto2, Satoshi Suzuki2 Ւ1CSIR-CFTRI, India, 2NFRI, NAROՓ
Common mode of asexual reproduction in fungi is by conidiation. Aspergillus oryzae is able to respond to light andpresence of conserved light related genes in genome sequence supports this fact. With this background, light regulation
with respect to morphology, growth and sporulation of A. oryzae were explored. A.oryzae were screened on potato
dextrose media and incubated at 30°C for four days illuminated under white light 10 min, a day along with control
which was maintained under dark condition. The preliminary experiments resulted in the colonies with circular stripe
pattern containing white and green rings which illustrated poor and rich spores and mycelia formation. The color of thecolony was much heavier in the white light condition than in dark. The aerial hyphae in the light condition were muchdenser than those under dark conditions. A.oryzae strain MSL1produced the fewest conidia under the dark condition
and the most under white light, suggesting light could stimulate conidiation. Strain MSL1 exhibited 1.94 fold moreasexual spores with light induction than with continuous dark. Inoculation on the surface of liquid minimal media also
demonstrated the sporulation to be more prominent in case of continuous light illumination than in dark. Thus theresults indicate that A.oryzae perceives and responds to light as a trigger of conidiation. Molecular mechanisms of photo
reaction of this fungus would provide physiological significance for basic and also for biotechnological processes.

 36 —P-3ՊёІű|¨¹¡¹ՒCAoGDՓS¹¹ʳʗOESĶͻБͼď 1Օ¼˄̩ƾ 3ՕǸ½ſѯ 1,2Ւ1 ӫІΧՕ2 ȎǺƺ¸ĝϊΧՕ3 ˗Țéΰ²ՓՊёՒAspergillus oryzaeՓTՕǍģȾ4Կ7Օ̽ӫjT@`OAfêϽΕΑӮԳƀbԳƀͻՕŐΐͻSӮϰSüϼ͈Օ=dRTՕ·ο·yҮ͹ͺS£O?Maùͻ=gՕɑ&S͹̭R˸7;OSįˆQ/Ȳ͹ͧN.f%ESӳѵȾ3dՕȡɕNՊёІű|¨¹¹¡¹(Comprehensive Aspergillus oryzae genome
database: CAoGD)j҅Г¸Ĥԃ?GՒhttp://nribf21.nrib.go.jp/CFGD/Փ%;g]N RIB40 ¹¹RK/Mˀ¹
¹¡¹NTՕßSё˗|¨¹yr·S¦·zɆƬQPT AspGD RՕŰοƧԸ˅åNS¦oyµm´oRcfΑͲѾˊɆƬT NRIB Ace33v2 Rà¿=gfQPՕEgFgͫχ?Mɾһ?M/G%E;NՕ
ŰοSɆƬjºɨ?MԆѺN5fc0RՕ¹¹¡¹ԄNĥӍ?MǉƞAfӟêǇRK/MՕʶʗSm
¹¯·jěR?M¹¹jϽű?ՕʇƊjƘJG%]GՕ;g]NRȡΧσǖNՊёS̎Һ|¨ѾˊRͻ/G̽ӫՕżƎՕӰ̟ͻQPS 55 Պё˗S|¨m´oSϹˌjɾһ?Օ¹¹Sm¹
jѦJG%â¼RK/MՕϩͪёİǇ͹ͧǋ}·l´·SԃēRűiCMĤԃAfÏǓO?M/f%]
GՕ;gdS¹¹¡¹jùͻ?GѾˊSÐúRK/MaűiCMϵÝ?G/%ÜȫՕȡ¹¹¡¹
TՕ±s¹¨SƺѸ˱QʇϚjÏǓ?M2eՕ®¹¹SɈѷjŤʦ?MѦ7ɕǉN.f%;S˶éRȯùͻԫ/G¼NѵʻbʇƊ͚QPSȯɈѷjԫ9gUȍ/N.f%

Update and use of Comprehensive Aspergillus oryzae Genome Database (CAoGD)
Ken Oda1, Yasuo Uemura3, , Kazuhiro Iwashita1,2 (1NRIB, 2Hiroshima Univ.,  3Genaris Inc.)

P-4
ՊёSm§±¹͹ͺRԅ¿AfҸĩƔǇSŰο͙ϰ͈R29fϳЩħǯƞѾˊÜӴŢЂՕӷʽτƼՕͼÂͷȃՕʗҝǫȜՕÓżŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓՊёS··İѾӮϰ͹ͺRTՕ··İѾӮϰӟêǇЖjΛɶĸȯAfҸĩƔǇ AmyR O¦³¹ŦeӃ^ϪjĸȯAf MalR S 2 οSҸĩƔǇ4ԅ¿?M/f%A.nidulans R2/MՕAmyR 4̭ȾŎOŖғΕR˘λѦAf;ORŅ1Օ¦³¹ǉƞ½ceao¦³¹bz³}¹ǉƞ½Nӎb3R˘λѦAf;O4Ƭź=gM/f (1)%ՊёR2/MTՕ/BgS͙ϰ͈Rce AmyR O MalR S˘λѦ2cW̭ȾŎ4ʟ7ҎǨ=gfS3¾ʣN.f%ˀΧσNT AmyR O MalR S̭ȾŎ˶ˬjѾˊAfG`Օz³}¹
ɛĸĸȯƔǇ (CreA) ΩƳ˗R29fΑͲѾˊ2cWŰο͙ϰ͈ƧԸʪS sGFP-AmyR O sGFP-MalR SϳЩħǯƞѾˊjѦJG%Űο͙ϰ͈R29fϳЩħǯƞѼǡSϹˌՕsGFP-AmyR TҎǨƨҮԥǉƞ½NTϳЩҮRǉƞ?M2eՕҎǨƨҮýǉΕR˘ǯƞAf;O4ʣd3RQJG%]GՕ¦³¹ceao¦³¹4ӎb3R
AmyR S˘λѦjҎǨAf;O4ʣd3RQJG%ºʘՕsGFP-MalR Tкż̹/;ORғZGģMS͙ϰ͈ƧԸʪR2/M˘ǯƞ?M/G%;S;O3dՕMalR ṰȾŎ¸ԥ̭ȾŎͪɋRԅidBՕˬɐΕR˘ǯƞ
?M/f;O4ί=gՕҎǨƨҮýǉΕR˘ħNôd3SĆԷjŧ9M/f;ORcḙȾŎAfaSOɷ
Ǔ=gG%
ˀΧσT͹Χ ·¹'Ӏˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%1) Murakoshi et al ., Appl Microbiol Biotechnol. 94: 1629-1635 (2012)
Intracellular localization in various carbon source of transcription factors involved in amylase production in
Aspergillus oryzae
Yui Konno, Kuta Suzuki, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi
(Div.Biosci.Biotechnol.Future Bioind., Grad.Sch.Agric.Sci.,Tohoku Univ.) 37 —P-5Պё΂Ԧ̭Ⱦ·yҮ hydrophobin RolA SΉ̒ȾѫԦYSŷΠ˶ˬSѾˊ̓ǵɂЕ 1ՕͼÂɦʾ 1ՕͼӣȜ̊ 1Օ¼ŞďÑ 1ՕԿ˵ȵ 2Օʸͼξȣ 3Օ˯ũĽȹ 3ՕԊӧʍɄ 1,2
Ւ1 ˈŏƺԍ¸ӀՕ2 ˈŏƺ¸ʾˆΧՕ3 ˈŏƺ¸ƹěΧՓAspergillus oryzae T͹İѾȾ¥²r³N.f PBSA(Poly(butylene succinate-co-adipate))jƆºS͙ϰ͈O?MƧԸAfOՕPBSA İѾӮϰS cutinase CutL1 OĥRՕ΂Ԧ̭Ⱦ·yҮN.f hydrophobin RolA jΑͲAf%RolA T PBSA RŷΠ?GȫՕCutL1 j PBSA ѫԦR²y³¹Af;ONՕPBSA SİѾňͯj¼ʢ=CM/f%hydrophobin TES΂Ԧ̭ȾͨȾRceՕ˃ʔѫԦŅȀYSȺͻ4ʼȩ=gM/f%ESºʘNՕ˭&QͨȾjʸAfƙóѫԦO hydrophobin OSΜÒöͻ˶ˬbՕŷΠSӎȑҕΕȾҮRK/MSҋϳT¾ʣN.f%Ͳƞ]NRɑ&TՕSAM (Self-Assembled Monolayer)ŎRcJM·QfȾҮSѫԦjöѱ?Օ
ESѫԦO RolA OSѻſȾj QCM (Quarts Crystal Microbalance)NͅǓ?MՕƙóѫԦSȾҮRcJM RolAŷΠSŊŃǋΕȾҮ4·Qf;Ojѷį?G%QCM jͻ/G RolA SŷΠѾˊNTՕQCM ͻ ·¹ӶԠ˪ѫԦSƢºQ SAM Ŏ4ȷѵOQf%E;NˀΧσNTՕɶѿѽͅǓO AFM (Atomic Force Microscope)jͻ/MՕQCM Ԡ˪S SAM ŎSȢɐͪɋj҈þAfʘ̥SέχjΚɫ?G%ɶѿѽͅǓO AFM ѼǡRceՕ1-undecanethiol Nöѱ?GΉ̒Ⱦ SAM ŎѫԦTƢºRöѱN5M/f;O4έҍ=gG%E;NͲƞՕƢº
Q 1-undecanethiol SAM ŎѫԦRǣ?MՕ·Qf pH SЋѩ̶˅å½N RolA jŷΠ=CGѫԦjöѱ?ՕAFM
NѼǡ?M/f%ѫԦѼǡSϹˌO QCM jͻ/GΉ̒ѫԦYS RolA SѻſȾѾˊSϹˌj̎ҺAf;ONՕΉ̒ȾSƙóѫԦRǣAf RolA SŷΠ˭Ț¸ŷΠ˶ˬjЛǡAf%
Analysis of adsorption mechanism of Aspergillus oryzae hydrophobin RolA to hydrophobic surface.
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 (O-3)
Պё hydrophobin RolA O¥²r³ԄSΜÒöͻR29f Cys7-Cys8 ³¹Sԅ¿ͼÂɦʾՒˈŏƺԍ¸ӀՓՕӶĚŝՒˈŏƺԍ¸ӀՓՕͼӣȜ̊Ւˈŏƺԍ¸ӀՓՕ¼ŞďÑՒˈŏƺԍ¸ӀՓՕƺԲʭǇՒˈŏƺԍ¸ӀՓՕԿ˵ȵՒˈŏƺԍ¸ʾˆΧՓՕԊӧʍɄՒˈŏƺ¸ʾˆΧՓhydrophobin TϩͪёRȎ7Ąǉ=gM/f΂Ԧ̭Ⱦ·yҮN.eՕ8 KSĄǉ=gG Cys ̄ƨjɪK%
Cys3-Cys4 ³¹šW Cys7-Cys8 ³¹TΉ̒ԦjȢɐ?ՕΉ̒ȾѫԦYSŷΠRԅ¿?M/fOЛ1dgM/f%͹İѾȾ¥²r³ polybutylene succinate-co-adipate (PBSA)jŶ_̶óƧƠNՊё Aspergillus oryzaejƧԸAfOՕPBSA YSŷΠȾjɪK hydrophobin RolA OՕPBSA İѾӮϰN.fy¹ CutL1 jİ̤
Af%RolA T PBSA RŷΠ?GȫˬӏƷŎ?ՕCutL1 j²y³¹Af;ON PBSA İѾjĂӑAf%
ˀΧσR2/MՕɑ&T PBSA YS RolA ŷΠwnyjՕ³p·m ošW Quartz Crystal
Microbalance(QCM)RcJMѾˊ?G%]GՕRolA SΉ̒Ⱦ³¹ÂRǉƞAfΉ̒Ⱦm§ӯ̄ƨjՕѻ̒Ⱦm§ӯS Ser RГɺ?GƷ·ójöѱ?ՕPBSA RǣAfŷΠwnyjѾˊ?G%Cys7-Cys8 ³¹
ÂS Leu137, Leu142 jГɺ?G RolA Ʒ·óNTՕӴ͹ƣ RolA O̎Һ?M PBSA YSŷΠӎȑ]GTʶƺŷΠӵ4ï½?G;O3dՕ;S 2 KS̄ƨ4 PBSA YSŷΠRӳѵN.eՕCys7-Cys8 ³¹4ŷΠRÄ
Rԅ¿Af;Ojίƅ?G%ͲƞՕCys7-Cys8 ³¹ÂSюԠȾm§ӯjΉ̒Ⱦm§ӯN.f Ala RГɺ?GƷ·ójͻ/ՕCys7-Cys8 ³¹ÂRǉƞAfюԠ4 PBSA YSŷΠRš\AȦԪjғZM/f%
Involvement of C7-C8 loop of Aspergillus oryzae hydrophobin RolA in interaction between RolA and a polyester.
Takumi Tanaka (Grad. Sch. Agric. Sci., Tohoku Univ.), Yoonkyung Kim (Grad. Sch. Agric. Sci., Tohoku Univ.),
Hiroki Tanabe (Grad. Sch. Agric. Sci., Tohoku Univ.), Kenji Uehara (Grad. Sch. Agric. Sci., Tohoku Univ.), Toru
Takahashi (NICHe., Tohoku Univ.), Keietsu Abe (NICHe., Tohoku Univ.).

 38 —P-7Պё hydrophobin RolA O cutinase CutL1 ԄSΜÒöͻRԅ¿Af CutL1 Sm§ӯ̄ƨӶ Ěŝ 1, Ǣħ ѯҧ 2, ͼÂ ɦʾ 1, ǧԻ ѯҏ 1, ¼Ş ďÑ 1, Կ˵ ȵ 3, Ԋӧ ʍɄ 1,2,3
Ւ1 ˈŏƺԍ¸͹ͧͺ˩Łɐ, 2 ˈŏƺ¸Ӏ, 3 ˈŏƺ¸ʾˆΧՓ Aspergillus oryzae j͹İѾȾ¥²r³N.f PBSA jƆºS͙ϰ͈O?MƧԸAfO, hydrophobin
RolA O PBSA İѾӮϰ cutinase CutL1 jĥΑͲAf%PBSA RŷΠ?G RolA T CutL1 OΜÒöͻ?, PBSAѫԦR CutL1 j͕ЎAf;ON PBSA İѾjĂӑAf%;g]NSΧσRcJM, RolA O CutL1 SΜÒöͻ
RTot·ΕΜÒöͻ4ԅ¿?, RolA ĐS H32, K34, K41, K46, K51 O CutL1 ĐS E31, D142, D171 4ϹűRӳѵN.f;O4ʣd3RQJG%?3?, QCM(Quartz Crystal Microbalance)jͻ/MŊŃǋΕѾˊjѦJGO;h, NaCl ǉƞ½R29f RolA ÑӳƷ·ó(H32S/K34S)RǣAf CutL1 »ӳƷ·ó(E31S/D142S/D171S)SϹűӵ4 NaCl ԥǉƞʪR̎ZԱјŔǪ?G%;S;O3d, ;g]NRͨǓ=gGӧîâƸRaot·ΕΜÒöͻӧî4̄ƞAfūЫȾ4ίƅ=gG%E;NˀΧσNT CutL1 ĐRΠΚ?, E31, D142, D171 âƸS
RolA OSΜÒöͻRԅ¿AfӧîjͨǓ?, ΜÒöͻ˶ˬjѾʣAf;OjΚΕO?G%CutL1 χóˬӏª
³O CutL1 £ªµzԄSm±o·©·Ѿˊ3dΜÒöͻRԅ¿AfOɷͅ=gfҡԠюm§ӯ̄ƨj
ʗGRӞɞ?G%ˀƬźNT, ĊѰӧîS0I D73 jԥюԠȾS Ser RГɺ?G CutL1 ºӳ, ƒӳƷ·ójöѱ?, QCM 2cW Pull-down assay Rce RolA OSΜÒöͻRK/M˧҇jѦJG%ESϹˌ, CutL1 D73 a
RolA OSϹűRӳѵN.e, ßSӧîOSƹþňˌRce RolA OSΜÒöͻRԅ¿Af;O4ί=gG%
Analysis of cutinase CutL1 amino acid residues involved in the interaction between fungal hydrophobin RolA and CutL1
Yoonkyung Kim1, Yuki Terauchi2, Takumi Tanaka1, Yusei Tsushima1, Kenji Uehara1, Toru Takahashi3, Keietsu Abe1,2,3(1Grad. Sch. Agric. Sci., Tohoku Univ., 2Dept. Agric., Tohoku Univ., 3NICHe., Tohoku Univ.)P-8̒ȾÑΜİө̥ՒATPSՓRcfՊё Aspergillus oryzae ͽˆ Hydrophobin HypA Sİԝ¸͕Ў¨SˬϚÂӴǐҷՕˁʘȔѯՕƪļƟòՕŅ͖ʣʜԺՕÂǺʧϲՒʣ̠ƺԍ¸Ӏ¸ӀŎՓHydrophobin OTՕϩͪё¸ɣǇёԲSϳЩѫǴRǯƞAfÁѻǆȾïİǇӵ·yҮN.eՕƨ˃ѫԦRŷΠ?Mѻ̒ȾjӊҸ=CfQP®¹yQȾҮjɪK;O3dՕ=]>]QİӴYSȺͻ4ʼȩ=g
M/f%?3?ՕHydrophobin T5i`MŷΠ¸ӳű?bA/¼RĨѾԝ4ƖԞQG`ՕΫǍ̉̚QPS͕̉̚Ў4¾ūЫN.eՕES¼[OkPSot·×ɺu±¨NTŷΠ?G]]͋į=gQ/G`ՕƓť¸Ϧѱ4ԥȉRƖԞN.f%ϐМdTՕՊё Aspergillus oryzae 3d Hydrophobin j}¹AfOЛ1dgfӟêǇ(hypA~D)jŘԝՕŰ&SӟêǇRK/MǯƞȾbΑͲʪʼSѾˊjѦQ/ՕHypA/RolA 4ƙóƧԸʪRʶaƹ7ΑͲ?M/f;OjѼǡ?M/f%ϐМdTՕՊё A.oryzae jǛÄO?G HypA ԿΑͲ˗j̶óƧԸ?ՕƧԸ¼̽jƓť?G%ԥot·Ⱦ΂Ԧ̭Ⱦľ Triton X-114 j 3%(v/v)̼Ņ?ՕԤГ?GO;hՕ̒ΜO Triton X-114 ΜRİԝ?ՕŘӵóS HypA
4 Triton X-114 ΜR͕Ў=gf;Ojѷ/H?G%;S Triton X-114 ΜRT̒İaİө=gM2eՕTriton
X-114 Μjİ̶?Օo¹³j̼ŅAf;ON Triton X-114 jԎşAf;ORceՕHypA S͕Ў̶̒͋jȮf;O4N5G%=dRՕԐot·×ɺyµ¦z±n¹ՒCELLUFINE Q-500 m ;JNC CorporationՓjѦ0;ORceՕϝĀQ HypA Sİԝ¸͕ЎRɐń?G%
Construction of the separation and condensation system of Hydrophobin HypA from Aspergillus oryzae using
Aqueous two-phase system (ATPS).
Hiroki Nakano, Yasuhiro Kuchikata, Keisuke Domae, Asuka Kase, Harushi Nakajima(Dept. of Agricultural chemistry.Univ. of Meiji) 39 —P-9ϩͪёͽˆSĠ΋ƓӠ˶ЫȾ·yҮjͻ/GʗѸŐΐͻϢǇSԃΑñѠƺҧ 1, ͂ӢαӲϾ 2, ˉ˄Ժђ 2, Կ˵ɌƼӦ 3, Կ˵ȵ, ˄ƤĤщ 1, ΥÔɂǇ 2, ǿ¼ſЗ 2, ī˳ҧɐ 4,Կѷҏº 5, ԊǬԚʑ 5, δˀǋ 3, ԊӧʍɄ 1, 6 Ւ1 ˈŏƺԍӀ, 2 ˈŏƺԍŐ, 3 ˈŏƺ¸ŅՏΧ, 4 ǵȢƺʹ,5 ˈŏƺ¸ƹěΧ, 6 ˈŏƺ¸ʾˆΧՓӶǳϢǇTŐΐȺͻ4ʼȩ=gM/f4ՕԤЮħRɜ¿?GϢǇŜP4Ġ΋ȺϓRcJMТеQ
PSϳЃħΖϪRɲɱ=g˰ΕϷБYķӘN5Q/;O4Ғ԰N.f%ºʘՕɑ&Tͺ˩ϩͪёN.fՊёS΂Ԧ̭ȾѢΓҮ hydrophobin(RolA) RԅAfΧσjѦJM5G%ESȫՕɊˑȾϩͪё Aspergillus
fumigatus R2/M hydrophobin 4Ġ΋ȺϓƓӠ (³) ЫjʸAf;O4ί=gG%E;Nɑ&TՕ͹óħNǍǓQӶǳӯŎͧϢǇjՕϩͪёSʗѸ³ƔǇN.f΂Ԧ̭ȾѢΓҮ RolA NѬѶ?GʗѸ³ϢǇSԃΑjѦJG%ӶǳϢǇTԿ̈́̒͢ŤȺRceűɐ?GӯŎӸ (Fe3O4) ϢǇ(ȋƢϢȨ 200 nm) jͻ/G%]BՕ¦pͽˆS˴ͪϳЩ2cW¦yµl¹jͻ/M in vitro NS
RolA ѬѶϢǇS³Ыj҈þ?G%ϹˌՕ˴ͪϳЩ3dSouo·ͺ͹Օ¦yµl¹RcfҤ
Գjț5ұ;=Q3JG%=dRՕ¦pR RolA ѬѶϢǇjɜ¿?GO;hՕТеYSϢǇњς4ǪQ7
͹óħNa³ЫjέҍN5G%]GՕRolA ѬѶϢǇS¹ԠîSͅǓϹˌ3dՕRolA ѬѶϢǇT
͹óħS pH ԮƦR2/MҡSԠîjʸ?M2eՕѥÂNSԿİʌȾ4Ïɇ=gf%
Development of imaging nano-particles coated with immune-response free (stealth) fungal proteins
Daiki Sato1, Yurie Watanabe2, Kana Matumura2, Shintaro Takahashi3, Kimihide Muragaki1, Ishi Keiko2, Kazuyoshi
Kawakami2, Takanari Togashi4, Seiichi Takami5, Masafumi Ajiri5, Manabu Fukumoto3, Keietsu Abe1, 6(1Grad Sch Agric Sci Tohoku Univ, 2Grad Sch Med Tohoku Univ, 3IDAC Tohoku Univ, 4Sci Yamagata
Univ.5IMRAM Tohoku Univ, 6NICHe Tohoku Univ)

P-10
Պё A. oryzae Sr±¹o·¹˭·yҮǵ½ ìԙ 1ՕȋˉρÅф 2, ǁ˄ ˺ͽ 2, ǩ˥ ͽЕǇ 2, ɘΡ ɂº 2,ʣΥ ҧѯ 1, ǩǿ ҬÑ 3, Ñʇ ăω 2

 Ւ1 ΓՅӫӏեΧσ, 2 Ŵƥƺџ, 3ՒͫՓˈŴŪǱΎԍՓ
ɑ&TՕʜſѷɊˑȾjaK Aspergillus fumigatus 3dʗѸQr±¹o·¹jŘԝ?ՕESˬӏRK/MѾʣ?G%K6Rͺ˩¼ʸͻQϩͪёN.fՊё A. oryzaeRIB40 3dՕr±¹o·¹
˭ͧҮ AOEI jŘԝ?Gդ ;SͧҮT gene dosage ňˌϑRcfԉṷ̈́ȾS¼ʢTѷdgBՕo·¹Sƺӵ͹ͺRcfǕͻŎՕX ЉˬӏѾˊϑjĄ΄?G%˹R A. oryzaeRIB40 3d AOEI OT·QfͧҮN.
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Elastase inhibitor-like protein from koji mold Aspergillus oryzae.
Nobuo Yamashita, Honoka Hiramatsu, Yoshiyuki Okumura, Yumiko Komori, Kei-ichi Uchiya, Takahiro Akashi, Kenji
Ogawa, Toshiaki Nikai(Hakutsuru Sake brewing Co. Ltd., Meijo Univ., Higashi Nagoya Nathonal Hospital) 40 —P-11Պё A. oryzae R29ft¹l¹ԅӐг·yҮ AoAtg9 SѾˊѠʽОȋՕѐԄԒȹՕŏˀŌV;Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓ)ΚΕ*t¹l¹TÑӳгˬӏjɪKt¹l~¹¨jÝ?MϳЩħɐİj²¹¨/̶ЩNİѾAf˶ˬN.eՕΟ˘͹ͧRȎ7Ąǉ=gM/f%ӄȌՕt¹l~¹¨Ȣɐ˶ˬRK/M̭ΑR
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Analysis of the autophagy-related membrane protein AoAtg9 in Aspergillus oryzae
Kohei FujikiՕTakashi KikumaՕKatsuhiko Kitamoto(Dept. of Biotechnol.ՕUniv. of Tokyo)

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Discovery of novel ribosomal peptide biosynthetic pathway in filamentous fungi
Myco Umemura1, Nozomi Nagano1, Hideaki Koike1, Koichi Tamano1, Keietsu Abe2, Kazuo Shin-ya1, Kiyoshi Asai3,
Masayuki Machida1(1AIST, 2Tohoku Univ., 3Univ. Tokyo) 41 —P-13³±¹ӟêǇj¦³}¹ǨĢ?GՊёSӟêǇ}¹ʎO
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Gene copy number and enzyme activity of Aspergillus oryzae strains constructed by introducing cellulase genes
Satoshi Wakai1, Nanami Asai1, Ryosuke Yamada1, Chiaki Ogino2, Hiroko Tsutsumi3, Yoji Hata3, Akihiko Kondo2(1Org. Adv. Sci. Tech., Kobe Univ., 2Dept. Chem. Sci. Eng., Grad. Sch., Kobe Univ., 3Res. Inst., Gekkeikan)




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1) Nemoto et al. (2009) Appl. Microbiol. Biotechnol. 82:1105-14.
Identification of a mutation involved in hyper-production of heterologous protein by comparative genomics inAspergillus oryzae
Feng Jie JIN, Jun-ichi MARUYAMA, Katsuhiko KITAMOTO (Dept. of Biotechnol., Univ. of Tokyo) 42 —P-15
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Overexpression of heterologous genes in deletion strains of genes involved in carbon catabolite repression in
Aspergillus oryzae
Sakurako Ichinose, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi
(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ.)P-16ՊёϳЩƲSαz³u·űɐRԅifƹӳӟêǇΩƳ˗SȢɋ2cWͧҮ͹ͺͨȾȟʖˆՕͼÂͷȃՕʗҝǫȜՕÓżŌË ˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՊёTĶͻįˆfӞɟ¦¹u¹4ԌdgM/fG`ƹӳӟêǇǨĢ2cWΩƳ4ƖԞN.JG%ɑ&TՕ
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Silai Zhang, Mizuki Tanaka, TakahiroShintani, KatsuyaGomi (Grad. Sch. Agric. Sci., Tohoku Univ.) 43 —P-17 (O-1)
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Characterization of the deletion mutants of pectin methylesterase genes in Aspergillus luchuensis.
Osamu Mizutani, Dararat Kakizono, Jin Shun, Toru Takahashi, Osamu Yamada (NRIB)

P-18 (O-4)ՊёϳЩȀƭjͻ/G L-2cW D-ÌӯS͹ͺϏćΛË 1ՕчÔʱ 2Օ̯Ôђ&Ǖ 2ՕяӴŒη 1Օƫ̱Ǉ 3Օι̫Ñ 3ՕӄѠʩȣ 1Ւ1 βɓƺ¸ȀՕ2 βɓƺ¸з͞θǋՕ3 ʷ˜Ī¸ІΧՓ)ΚΕ*ˀΧσSΚΕTՕՊё Aspergillus oryzae jͻ/G··3dS L-2cW D-ÌӯS͹ͺN.f%ÌӯTՕȭˆS±yϑRʵifot±yN.f¥²ÌӯSŞʔOQf%L óO D ó4̻
ű=gG´t}·´yƣ¥²ÌӯTН͢Ⱦ4Կ7ՕESG`ՕL-2cW D-ÌӯÁʘSԡѵ4ìW
M5M/f%ՊёTϳЩƸRјӵSm§±¹jİ̤AfSN··İѾЫ4Կ7Օ··3dSÌӯ͹ͺSʸͻQ£SºKOЛ1dgf%)Ϲˌ2cWЛǡ*A. oryzae S|¨¼S lactate dehydrogenase (LDH)ӟêǇj˸ƿ=CՕÌӯ͹ͺЫ4Կ/ͥͽˆ LDH jǨĢ?, Łɐ?GȢҮҸɺՊё A. oryzae LDHΔ871 T, 100 g/L ū͋Ⱦ··3dϬ 30 g/LSÌӯj͹ͺ?G%͹ͺ=gGÌӯSĞǋϮȑTՕ99.9%â¼4 L óN.JG%]GՕ¼҄OTĵR A. oryzae
RՕ»οSȲ͹ͧͽˆ D-lactate dehydrogenase ӟêǇSȢҮҸɺjѦJG%Łɐ?GȢҮҸɺóSº˗TՕ100
g/L ··3d 23 g/L S D-Ìӯj͹ͺ?G%͹ͺ=gGÌӯSĞǋϮȑTՕ99.9%â¼4 D óN.JG%
â¼Օ Պёjͻ/f;ON··3dS L-2cW D-ÌӯS͹ͺRɐń?G%ºʘNՕES͹ͺӵTz³}¹3dS͹ͺӵO̎ZMï/%ÜȫTՕáҚʇƷϑRce͹ͺňͯSŵ¼jΚɫAOĥRՕ··
H93dNQ7 ³µ¹ot¦3dS L-2cW D-Ìӯ͹ͺjΚɫA%
Production of L- and D-lactate in Aspergillus cell factory
Naoya Sasakura1, Satoshi Wakai2, Nanami Asai2, Chiaki Ogino1, Hiroko Tsutsumi3, Yoji Hata3, Akihiko Kondo1(1Dept. Chem. Sci. Eng., Grad. Sch., Kobe Univ., 2Org. Adv. Sci. Tech., Kobe Univ., 3Res. Inst., Gekkeikan) 44 —P-19
t´o·ӯšW²¹³ӯԿ͹ͺjΚΕO?G Mortierella alpina SİǇХοԇˀՆѦ 1Օ˷ҝщ̠ 2ՕǍѠʫѸ 3ՕǺ Ϯ 4Օǩǿ Ԭ 1,3
Ւ1 ÙƺԍӀեȺͻ͹žՕ2 ȳǺƺԍեȀՕ3 Ùƺ͹ʹ®Օ4 ՐҝƺՓ)Чʭ*̟ЬT͙Ŏ̒ϰԾ˚jʸAfԿӡěȑŎűͧN.eՕͲʸAfŎǋȀ˩R29fΥ̟áʵŞʔO?
MʸͻN.f%ͨRՕt´o·ӯՒ18:1ω9, OAՓšW²¹³ӯՒ18:2ω6, LAՓT̒ӯŎͧjϸMoµ· 6¸
10 ¥²¦¹SŞʔN.f ·ӯYOƷɺūЫN.f%ϩͪё Mortierella alpina TЬҮjƹӵRњςAf
ȾҮjʸAf̟ϨȲ͹ͧN.f4ՕESЬФӯϷɐTƹǶRiGf%ˀΧσNTՕµzm·ĮʹjѦJG M. alpina Û͛υ͞Ʒ·˗Жce Δ12 ¾ԶſŎӮϰՒDSՓ̭Ⱦ˸ɽ˗šW Δ6DS ̭Ⱦï½˗jӞɞ?Օ;gdSİǇХοRce=dR OA šW LA jԿњςAfƷ·˗SҎǨj҉^G%)Ϲˌ*Δ12DS ̭Ⱦ˸ɽ˗ЖR2/MՕOA jІЬФӯȡGe 50%ӄ7͹ͺAf OA Կ͹ͺ˗jӞɞ?G%=dRՕOA Կ͹ͺ˗R2/MՕmzµy²p¨̥jͻ/M Δ6DS ӟêǇS RNAi jѦJGϹˌՕ§¹ӯ͹ͺSï½RëJM OA Ŷʸӵ4 60%j¼ƓfİǇХο˗4ȮdgG%ų˭RՕΔ6DS ̭Ⱦï½˗ЖceՕ
LA 4ІЬФӯȡGe 25%ӄ7њςAf LA Կ͹ͺ˗jӞɞ?G%=dRՕLA Կ͹ͺ˗R2/MɣǇё
Coprinopsis cinerea ͽˆS Δ12DS ӟêǇjӖĿΑͲ=Cf;ORceՕOA ŶʸӵSï½RëJM LA Ŷʸͯ
4 45%R]N¼ʢ?GİǇХο˗jȮG%
Molecular breeding of Mortierella alpina for high-production of linoleic acid and oleic acid
Takaiku Sakamoto1, Eiji Sakuradani2, Akinori Ando1,3, Jun Shima4, Jun Ogawa1,3(1Div. Appl. Life Sci., Grad. Sch. Agric., Kyoto Univ., 2Fac. Eng., Tokushima Univ. 3Res. Unit Physiol. Chem. Kyoto
Univ., 4Ryukoku Univ.)

P-20
Pythium sp.ͽˆ ω3 ¾ԶſŎӮϰӟêǇj̭ͻ?G̟ϨȲ͹ͧ Mortierella alpina 1S-4
Rcf EPA Sȉ̈́͹ͺǍѠʫѸ 1, 2ՕÂӂҔȋ 2ՕѐǿǠŭ Օ˷ҝщ̠ 3ՕǩǿԬ 1, 2Ւ՘Ùƺ¸͹ʹŎǋ®ՕՙÙƺԍ¸Ӏ¸Ⱥͻ͹žՕ՚ȳǺƺԍ¸tՓ)Чʭ¸ΚΕ*m±w·ӯ͹ͺȾϩͪё M. alpina 1S-4 TՕï̈́˅å½NƧԸAf;ONro}¢·r·ӯ(EPA)jњςAf;Oi3JM/f%;g]NRՕˀёSİǇХοjӍ@MЬФӯϷɐSʇƷjƬź?M
5G%ˀΑѫNTՕß͹ͧͽˆS ω3 ¾ԶſŎӮϰӟêǇjˀёRǨĢAf;ORceՕȉ̈́½R29f EPA͹ͺЫj҉^GSNƬźAf%)ʘ̥¸Ϲˌ*ϩͪё Pythium sp.ͽˆ ω3 ¾ԶſŎӮϰӟêǇS}·ùͻԯȑj M. alpina ˭RʇƷ?ՕԿ
ΑͲµª¹¹RMĸȯ?GΑͲu jˬϚ?G%ˀΑͲu jp±³ѵ̔Ⱦjɫ˰OAf¦¹u¹ӟêǇO·¨RӐϹ?Go²¹¡y¹jˬϚ?Օmzµy²p¨̥RM M. alpina
1S-4 RǨĢ?G%ǍǓQȢҮҸɺ˗jӞɞȫՕ5 ml S GY ƧƠՒz³}¹ 2%ՕӮ̋rw 1%Փjͻ/M
28 ºC NSȉ̈́ƧԸjѦJG%ЬФӯjɢįȫՕvyµ¦z±n¹RMİˊ?GO;hՕƸˆӟêǇN.f ω3 ¾ԶſŎӮϰSΑͲRcf ω3 ϪЬФӯњς4έҍN5Օ7 ʜԄƧԸR2/MՕЬФӯ͹ͺӵTϬ 0.4
mg/mLՕEPA ŶʸͯTІЬФӯÂSϬ 20%RӘ?G%EPA production under room temperature by Mortierella alpina 1S-4 introduced omega-3 desaturase genederived from Pythium sp.
Akinori Ando1, 2, Ryohei Nakatsuji2, Hiroshi Kikukawa2, Eiji Sakuradani3, Jun Ogawa1, 2 (1Res. Uni. Physiol. Chem.,
Kyoto Univ. 2 Div. Appl. Life Sci., Grad. Sch. Agric., Kyoto Univ. 3 Inst. Technol. Sci., Univ. Tokushima) 45 —P-21
ϩͪё Pythium sp. ͽˆ ω3 ¾ԶſŎӮϰӟêǇSӮ̋ΑͲϪjͻ/G˶ЫѾˊѐǿǠŭ 1ՕÂӂҔȋ 1Օ̯Ôƺҧ 1Օ˷ҝщ̠ 1,2ՕǍѠʫѸ 1,3ՕǩǿԬ 1,3 (1 ÙƺԍӀ¸Ⱥͻ͹žՕ2 ȳǺƺԍ¸
tՕ3 Ùƺ¸͹ʹŎǋ))Чʭ*ω3 ЬФӯTՕɝ͘ΏöͻQPƹȤQ͹ʹ˶Ы4Ƭź=gՕŐџ¸ďȔԳƀO?Mԡѵ4Կ]JM/
f%ͲƞՕω3 ЬФӯ͹ͺTՂ̟Rýǉ?M2eՕǍǓüϼ͈O?MȲ͹ͧSХοRcfáʵ͹ͺ4˧҂=g
M/f%ˀΧσNTՕω6 ЬФӯ3dS ω3 ЬФӯ͹ͺSӼӮϰN.f ω3 ¾ԶſŎӮϰՒω3DSՓӟêǇSŘ
ԝO˶ЫѾˊjѦJG%)Ϲˌ*ƜƴceŘԝ?Gro}¢·r·ӯ͹ͺȾϩͪё Pythium sp.ceՕӄЌοS ω3ds ӟêǇSm§ӯΜųөĲjaORЎӳ±o¦¹j҅ҁ?ՕˀёS|¨ DNA O cDNA jӺƣ
O?Gyµ¹·zjѦJG%ϹˌՕӄЌοS ω3DS OΜųȾjίA£ªµzӟêǇSƯƨөĲjŦȮ?Օ
369 ̄ƨSm§ӯ3dQf·yҮN.fOʣd3R?G%]GՕω3ds ΑͲӮ̋RMˀӟêǇSΑͲѾˊjѦJGϹˌՕω6 ЬФӯjǣȺAf ω3 ЬФӯYOƷɺAf ω3 ¾ԶſŎ̭ȾjίA;O4έҍ=gG%

Characterization of an omega-3 desaturase gene from Pythium sp. by using yeast expression system
Hiroshi Kikukawa1, Ryohei Nakatsuji1, Asai Takahiro1, Sakuradani Eiji1,2, Akinori Ando1,3, Jun Ogawa1,3 (1Div. Appl.
Life Sci., Grad. Sch. Agric., Kyoto Univ. 2Inst. Technol. Sci., Univ. Tokushima 3Res. Uni. Physiol. Chem., Kyoto
Univ.)

P-22ÛȀy´m¹ TALENs jͻ/Go/aIΎёR29fԿňͯӟêǇʇƷ̥э̼ҧÇ 1ՕǩǿƃË 1ՕƺӲĆº 1ՕñÆԄƃŭ 2Օǵˀŕ 2Օʸ̖Ń 3Օ˞ͼъ 1 Ւ1 ʣ̠ƺԍӀ¸2 ȎǺƺԍʹ¸3 ӀȀƺԍӀՓ
DNA ÑˀӾıʕ (DSB) ĆȰ˶ˬjĶͻ?MՕ˰ΕӟêǇħYSƯƨГɺՕ˸ƿbɰĢQPjÛ͛ΕRҎ
ǨAf|¨ЊԛəѧTՕæɈSƯƨөĲͨ·ΕR DSB jǨĢAf;O4ūЫQÛȀy´m¹SԃΑR
ceӑǲ?KK.f%ɑ&TՕ˦ͧΎŞϩͪёN.fo/aIΎёS DSB ĆȰ˶ˬSѾˊϹˌjaORՕ
Platinum Gate TALEN ¨ (Sakuma et al., 2013) SϩͪёYSʶӜŎOԿňͯӟêǇʇƷ̥Sέχj҉^G%]BՕģ CDS ԮƦjϩͪёS}·ùͻԯȑRʶӜŎ?G Platinum Gate TALEN ¨jˬϚ?G%
˹RՕ©±·͹űɐ͹ϸҴRԅif Scytalone dehydratase (SDH) ӟêǇj˰ΕO?G TALEN ¡y¹j
o·?ՕџľНȾӟêǇjŶ_ΩƳ¡y¹OSĥǨĢRceȮdgfӟêǇʇƷňͯ3d TALEN S DSB̭Ⱦj҈þ?G%TALEN OSĥǨĢRcJMȮdgGџľНȾ˗NTՕSDH ӟêǇ4ΜųϷɺ1jÝ?MΩƳ=gG;OjίAёŨSΓсŎ4Ѽǡ=gՕESňͯT 100%R]NӘ?G%â¼ce TALEN jͻ/GԿňͯ DSB SǨĢ2cWӟêǇʇƷ̥4ϩͪёR2/MʸͻN.f;O4ί=gG%
Highly efficient targeted gene replacement in the rice blast fungus using engineered TALENs
Takayuki Arazoe1, Tetsuya Ogawa1, Shuichi Ohsato1, Tetsushi Sakuma2, Takashi Yamamoto2, Tsutomu Arie3, Shigeru
Kuwata1(1Grad. Sch, Agric., Meiji Univ., 2Grad. Sch. Sci., Hiroshima Univ. 3Grad. Sch. Agric. Sci., Tokyo Univ. of Agric. &Tech.)

 46 —P-23̇ёľ¥²tw·НȾӟêǇSųǓ
œˀǒ 1Օ̣̬Ȝα 2Օŏįԙ͹ 1ՕͼÂŒǦ 1 Ւ1 ÙӨƺ¸ԍ¸ӀՕ2 ͍ҩΞχƺ¸͸ưθǋՓɝ͹ͧҮ¥²tw·TՕΟёϳЩƲj¹|OAḟёľNՕESöͻ˶öTƨҮ UDP-N-m ³z³}§·OSɩɝRcfw·űɐӮϰSԉǘOЛ1dgM/f%]GՕˀľSНȾ˶ˬO?MTՕџľSŦӃï½4 Alternaria ǳёNƬź=gM/f%ºʘՕBipolaris maydisՒpªµ}<]їˎΎёՓSυ͞Ʒ·˗jͻ/GǕԽ3dՕѲʎS¥²tw·НȾӟêǇ4ųǓ=gM2eՕџľSŦeӃ^âƸSН
ȾŎ˶ˬSǉƞ4ίƅ=gM/f%ÜƓՕ;gdНȾӟêǇS0IՕPol2 QdWR Pol4 RK/MՕģ|¨ɗ̥jͻ/MİǇӟêǋΕQųǓjѦJG%Q2Օ;gdSНȾӟêǇTՕџľНȾH9NQ7Օёϩ͹Х
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?ՕC410Y Sm§ӯГɺƷ·4ՕPol4 T Hydroxymethylbilane synthase (=Porphobilinogen deaminase)j}¹
? G241D Sm§ӯГɺƷ·4͹@M/f;O4Ĵʣ?G%;gdSӟêǇT/Bga ¨͹űɐϪSӟ
êǇN.fG`ՕƧƠR §·j̼Ņ?ՕНȾ˗ѫͲƣRǣAfȦԪjғZG%ESϹˌՕНȾ˗R^dgfёϩ͹ХSï½4ՕӧİΕRʇƊAf;O4i3JG%ͲƞՕ ¨͹űɐO¥²tw·НȾŎՕ.f/Tm·±w·њςSԅӐRK/MSѾˊjѦJM/fO;hN.f%
Identification of two polyoxin resistant genes in Bipolaris maydis.
Hiroshi Masumoto1, Kosuke Izumitsu2, Yuki Kitade1, Chihiro Tanaka1(1Grad. Sch. of Agri., Kyoto Univ., 2Sch. of Environmental Science, Univ. of Shiga Pref.)P-24˦ͧΎŞё Ustilago maydis R29fĳʼr·¹¨ŊɋS͹ʹǋΕɈЗRԅAfѾˊ˯ũ ѯ˹Ӧ 1, Gero Steinberg2 (1 Êƺԍ¸͹Ҫ͸¸͹ž˶ЫՕ2 ry

¹ƺՕ͹žθǋ)

r·o¹ϸҴR29ft³v±N.fĳʼr·¹¨NTՕϳЩг3dŦeӃ]gGu¹~4Ӟĵ=gՕϳЩгYOĨW²oy²·z=gf3a?7T²¹¨/̶ЩYOӉdgMİѾ=gf%
ˀΧσNͻ/G˦ͧΎŞȾSª³ÑȢɐӮ̋N.f Ustilago maydis jŶ`Gƹ7S͹ͧοR2/MTՕĳ
ʼr·¹¨TŊɋjίA%ESŊɋSİǇ©u¨T̎ҺΕр7Χσ=gM5G4ՕQDŊɋjίA
S3Rԅ?MT[\ʾ΢N.JG%ˀΑѫNTՕĳʼr·¹¨SŊɋSɈЗRǣAfºKSϓ1jɸ˝Af 1)%]B͹ϳЩR2/M²¤¹¨jūѹŎAfG`Օ40S 2cW 60S S²¤¹¨·yҮN.f
Rps3 O Rpl25 jӞWՕORF S½̮RѣĞ·yҮSӟêǇjѤű=CG%Rps3-mCherry 2cW Rpl25-GFP
T˘jԎ7ϳЩҮRѼǡ=gfaSSՕϳЩҮSºӧj FRAP (ĞӈсȫѣĞƓȰ) ѾˊAfOՕÁ·yҮSĥŊɋ4έҍ=gՕ²¤¹¨T 80S O?MŊɋjίA;O4i3JG%ESŊɋTȲǩϗՕw·¸
o·ª¹¹·yҮRýǉ?Օĳʼr·¹¨OĥŊɋjί?G%]GՕ´˅åb·yҮЙ҆ԉǘľjͻ/GѾˊ3dՕŊɋjίA²¤¹¨T·yҮЙ҆jѦJM2eՕ¥²¹¨jȢ
ɐ?M/f;O4ίƅ=gG%=dRՕ̈́ȑɊŧȾƷ·˗jͻ/Mĳʼr·¹¨SŊɋj˸ɽ=CfOՕ
¥²¹¨SϳЩħİȇR·ȉ4ѷdgG%;S;O3dՕĳʼr·¹¨SŊɋT¥²¹¨jϳЩħRƢºRİȇ=CfSRӳѵN.f;O4ίƅ=gG%1) Higuchi et al. (2014) J Cell Biol 204, 343-357.
Analysis of physiological significance of early endosome motility in the plant pathogen Ustilago maydis
Yujiro Higuchi1, Gero Steinberg2 (1Dept. of Biosci. Biotechnol., Kyushu Univ., 2Biosci., Univ. of Exeter) 47 —P-25pz°{SǇǕóʾɐ͡υ͞Ʒ·óSŞƔӟêǇT CHD1 £ªµzj}¹?M/G%˄ũ ěՕ΃Â;B1ՕǷӴ˜˴ ՒηͼΞχƺ¸͹ͧҪ͈ՓɣǇёpz°{SǇǕóȢɐӖνSΑ͹υ͞Ʒ·óSÂRՕ ǇǕóŞƨ4Ǫ?ɖȋOQeՕ Ǉ
Ǖóɐ͡4ұ;dQ/υ͞Ʒ·ó#1016 4.JG%#1016 ˗OӴ͹ƣº˘ёϩ˗ KF3#2 Oj×ө?ՕES F1
ǇǌSӟêǇƣjғZGO;hՕӴ͹ƣ՟υ͞Ʒ·ՠ41՟34 Rİԝ?ՕŘºSӟêǇRυ͞Ʒ·4ұ;JM/fOȼigՕESŞƔӟêǇȒj mal1 OŴà9G%¼҄ F1 ǇǌjùJM mal1 ӟêǇȒOӐӾAf RAPD¦¹u¹jɵ?GO;hՕώ III ˑсó¼S G4-3000B ¦¹u¹4Ϸɺ1ͯ 12.5ՑNӐӾ?G%˹Àá¹yr·¹jùJM#1016 ˗SģƯƨөĲj 1.4GbpՒϬ 30 ĉu¹ՓѾґ?Օώ III ˑсó¼NƷ·ӧîjɵ?G%ESϹˌՕӟêǇΆŮ CC1G_04478ՒCHD1 Μų·yҮ 1441 m§ӯj}¹ՓÂS 172 ΆΚS}· CAAՒQ:z³§·Փ4 TAAՒSTOPՓRƷ·?M/f;Ojѷį?G%;SӴ͹ƣӟêǇԮƦj PCR
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The gene responsible for a maturationless mutant of Coprinopsis cinerea encodes a CHD1 homolog.
Hajime Muraguchi, Kozue Hatanaka, Keiju Okano(Dept. Biotech., Akita Pref. Univ.)P-26ͦьĥ͹ϩͪё Epichloë festucae SïİǇӵ G ·yҮ Cdc42 2cW RacA SΜÒöͻƔǇͨ·ȾS˶ЫѾˊ˫ӴŢԺՕόˀƺŸ ՒŴƺԍ¸͹žӀǋՓ
 E. festucae ToθͦьOĥ͹ԅājέχAfϩͪёr·loN.f%;g]NRՕˀёSǛÄ˦ͧYSĥ͹ΕɊˑRTՕ̭Ⱦӯϰ͹ɐӮϰ NoxA 2cWESĸȯƔǇN.f NoxR OïİǇӵ G ·yҮ
RacA 4ȷѵN.eՕ;gdӟêǇSΩƳ˗TǛÄ˦ͧjˎ́=Cf;Ojί?M/f%NoxR TՕRacA RŅ
1ՕӮ̋NT˪Ⱦ̙ǓRԅ¿Af;O4΢dgf BemA 2cW Cdc24 OϹűAf;O3dՕ;gdƔǇSѲ
űó4 NoxA S̭Ⱦjĸȯ?M/fOɷǓ?M/f%]GՕRacA O˪`MԿ/ΜųȾjίAïİǇӵ G ·yҮ Cdc42 4 BemA Oͨ·ΕRϹűAf;OՕcdc42 ΩƳ˗4ǛÄ˦ͧYSģҶΕɊˑЫjƿ0;O3dՕ
Nox ѲűóOΜÒöͻAfÁïİǇӵ G ·yҮ4ǛÄYSɊˑR·QfȧŀjˌGA;OjƬź?G%
E;NՕRacA-NoxR 2cW Cdc42-BemA Sͨ·ΕϹűЫj̙ǓAfm§ӯjͨǓ?GO;hՕRacA S 32
ΆΚSm±·2cW 35 ΆΚSz²·4ՕCdc42 S 59 ΆΚSq³m±·4EgFgȷԭN.f;
O4ѾJG%m§ӯГɺRceͨ·ΕΜÒöͻjƷŎ=CG RacA 2cW Cdc42 jͻ/M racA ΩƳ˗SΜѰǕԽjѦQJGO;hՕNoxR OSϹṷ̋ȾjɪKƷ· Cdc42 RcJMՕracA ΩƳ˗Sĥ͹έχЫSƓȰ4ҍ`dgG%ºʘՕNoxR OSϹűȾjƿJGƷ· RacA NT racA ΩƳ˗Sĥ͹ЫjΜѰįˆQ3JG%;SϹˌ3d RacA O Cdc42 Sĥ͹έχR29f˶ЫİŎT 2 m§ӯөĲSә/Rcf NoxR ϹűȾRcJ
M̙Ǔ=gM/f;O4ί=gG%
Functional analysis of specific interactions between Cdc42-BemA and RacA-NoxR in fungal endophyte Epichloë
festucae
Yuka Kayano, Daigo Takemoto(Grad. School Bioagr. Sci., Nagoya Univ.) 48 —P-27ͦьĥ͹ϩͪё Epichloë festucae R29fёϩѤű˸ɽ˗SɵϱOĥ͹έχЫSѾˊǷ˄ʑԩՕͼÂɉǇՕόˀƺŸ ՒŴƺԍ¸͹žӀǋՓ

E. festucae ToθͦьRĥ͹ΕRɊˑAfϩͪёr·loN.eՕο&S´RǣAfǛÄ˦ͧSɡɝȾjŵ¼=Cf%E. festucae SǛÄ˦ͧYSɊˑRȷѵQƔǇO?MՕ̭Ⱦӯϰ͹ɐӮϰ NoxAՕ µ»ӵó G ·yҮ® GpaAՕ˶Ыʾ΢S˘·yҮ NsiA QP4ѷ/H=gM2eՕ;gdSӟêǇΩƳ˗NTǛÄ˦ͧOSųғΕQёϩ͹ХЫjƿ/ՕǛÄS͹Хjј?7ԉǘAf;O4ʣd3
RQJM/f%;g]NRŘԝ=gGĥ͹Ʒ·˗TAZMƧƠ¼NSёϩѤűЫjƿJM/f;O3dՕёϩѤűЫOĥ͹έχЫRTǝɶQԅā4.fOɷǓ=gG%E;NÜƓՕ±§ɰĢƷ·̥jͻ/MՕёϩѤűЫj˸ɽ?G RPA519 ˗2cW RPA112 ˗jŘԝ?G%]Gmu·uR2/MёϩSгѤűRΛɶ˶ЫAfOɷǓ=gM/fг·yҮj}¹Af Ham8 SΜųӟêǇj E. festucae 3dųǓ?ՕESΩƳ˗jöį?G%;gdё˗jǛÄ˦ͧRɶο?GO;hՕёϩѤű˸ɽ˗N.f RPA519 ˗ՕRPA112
˗2cW ham8 ΩƳ˗4Ɋˑ?G˦ͧSΤŎ4Ѽǡ=gՕE. festucae R29fёϩѤűЫOĥ͹έχ˶ˬSΜ
ԅ4=dRί=gG%ͲƞՕѤűƷ·˗NΩƳ=gM/fӟêǇSͨǓjӑ`M2eՕESϹˌRK/MaƬźAf%

Possible correlation between abilities of symbiotic infection and hyphal cell fusion of endophytic fungus Epichloë
festucae.
Okamura ayane, Aiko Tanaka , Daigo Takemoto(Grad. School Bioagr. Sci., Nagoya Univ.)

P-28
BiFC ̥jĶͻ?GՊё A. oryzae SёϩѤűSūѹŎOѾˊǷӧ΢ȝ 1ՕƮǼſ÷Ǉ 1ՕӶ ӹˇ 1ՕǸ½ſѯ 2ՕѠÔӥԙ 3ՕÃǵ͒º 1ՕŏˀŌV; 1Ւ1 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՕ2 ӫІΧՕ3 ԇȐƺԍ¸ʹՓϩͪёTёϩѤűjѦ/Օ}µ¹ȢɐR2/MёϩP0?S¶¹yjȢɐAf%]GՕёϩѤűTʸȾ͹̅2cWΊíʸȾ͹̅NSώº̆ԓN.eՕ×өХοjѦ001NӳѵQӖνN.f%ɑ&TʶӄՕՊё Aspergillus oryzae R2/MՕ2 KS˖Ըѵ̔Ⱦ˗jĶͻ?MёϩѤűjѾˊAfʘ̥jέχ?G 1,2)%?
3?Օ;Sɗ̥NT A. oryzae 4PS͹Х̆ԓNёϩѤűjѦJM/fS3RK/MѾˊAf;OTƖԞN.JG%ˀΧσNTՕBiFC (bimolecular fluorescent complementation)̥jĶͻ?MёϩѤű4ұ;JGϳЩjūѹŎ?ՕΛɶѼǡAf;ORce A. oryzae SёϩѤűЫŃRԅ?MѾˊjѦJG%
BiFC ̥RcfѾˊRTՕ µo¦¹O?MϹűAfc0R҅ҁ=gG·yҮ LZA 2cW LZB3)Օ
2cWѣĞ·yҮ EGFP jùͻ?G%A. oryzae SӴ͹˗ RIB40 RͽˆAf 2 ˗S·Qf˖Ըѵ̔Ⱦ˗R
2/MՕEGFP S N ʿĐO LZA jѤű=CG nEGFP-LZAՕEGFP S C ʿĐO LZB jѤű=CG cEGFP-LZB
jEgFgΑͲ=CՕÁ˗j̻ű?MƧԸ?G%ESϹˌՕёϩѤűRce˖Ըѵ̔Ⱦ4ΜѰ=gGϳЩR
2/Mͨ·ΕR EGFP ѣĞ4Ѽǡ=gG%;gRceՕA. oryzae R2/MёϩѤű?GϳЩjūѹŎAf;ORɐń?G%=dRՕѤű?GϳЩSȢɋjѾˊ?GϹˌՕİ͹ǇųƵ4Ѥű?Gƭű4aJOaƹ7Օ
mu·uNƬź=gM/f CATs (conidial anastomosis tubes)RcfѤűOԲí?M/G%ͲƞՕӱӏNù
igM/f A. oryzae ˗SёϩѤűЫjғZfG`ՕBiFC ̥Rcfų˭SѾˊjѦJM/f%
1) Wada et al. (2013) Appl. Microbiol. Biotechnol. 2) Tsukasaki et al. (2014) Biosci. Biotechnol. Biochem.
3) Kojima et al. (2011) J. Biosci. Bioeng.
Visualization and analysis of hyphal fusion by bimolecular fluorescent complementation in Aspergillus oryzae
Tomoya OKABE1, Wakako TSUKASAKI1, Feng Jie JIN1, Kazuhiro IWASHITA2, Ikuo FUJII3, Jun-ichi
MARUYAMA1, Katsuhiko KITAMOTO1 (1Dept. of Biotechnol., Univ. of Tokyo, 2NRIB, 3Osaka Pref. Univ.) 49 —P-29
Պё Aspergillus oryzae SёϩѤűR29f AoSO S˶ЫѾˊƮǼſ÷ǇՕÃǵ͒ºՕŏˀŌV;Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓϩͪёR2/MTºоRՕёϩѤűjӍ@Mų˗a?7T·˗4ΜÒRɶЁ=gG}µ¹jȢɐ?ՕE
gjӍ@MϳЩҮb˘S̻ű4ұ5fO=gM/f%]GՕёϩѤűTʸȾ͹̅ՕΊíʸȾ͹̅Sώº̆ԓ
Na.f%ɑ&TâļՕՊё Aspergillus oryzae R2/M˖Ըѵ̔Ⱦ˗jͻ/MёϩѤűňͯjǓӵΕRѾˊ
Afɗ̥jέχ? 1)ՕAoSO O/0ԔƲǈRĭԛ?͋ёSêʃjԈ8˶ЫjaK·yҮ 2)4ՕёϩѤűR
ȷԭN.f;Ojί?G 1)%AoSO T 1196 m§ӯ3dQfȁƺQ·yҮN.eՕC ʿĐ 641 m§ӯSԮƦ4͋ёSêʃjԈ8˶ЫRőİN.f;Ojί?G4ՕёϩѤűR29föͻ˶ˬRK/MT[OkPѾʣ=gMQ/%E;NÜƓՕAoSO S˭&QԮƦ˸ƿóΑͲ˗jĶͻAf;ORceՕESёϩѤűR
29f˶ЫRK/MѾˊ?G% AoSO SԮƦ˸ƿóΑͲ˗Rǣ? pyrG 2cW adeB ӟêǇΩƳjѦ0;ORceՕp²·/p±³Օm
·EgFgS˖Ըѵ̔Ⱦ˗jöѱ?G%̻űƧԸR29fёϩѤűRcJM˖Ըѵ̔Ⱦ4ΜѰ=gG
µu²t·SįͲͯjaORՕёϩѤűňͯjғZG%ESϹˌՕAoSO 4ԔƲǈͨ·ΕRĭԛAfSR
ȷѵQ C ʿϊ 50 m§ӯSԮƦ4ՕёϩѤűRaӳѵQ˶ЫjaK;O4ίƅ=gG%ºʘNՕAoSO S N
ʿĐ 555 m§ӯSԮƦT͋ёSêʃjԈ8˶ЫRȷѵNQ7Օ˶Ы4¾ʣN.f%ͲƞՕAoSO S N ʿĐSԮƦb;gRŶ]gf WW ©o·RK/MՕёϩѤűR29fȧŀjѾˊ?M/f%
1) Tsukasaki et al. (2014) Biosci. Biotechnol. Biochem. 2) Maruyama et al. (2010) Biochem. Biophys. Res. Commun.
Functional investigation of AoSO protein in hyphal fusion of Aspergiillus oryzae
Wakako TSUKASAKI, Jun-ichi MARUYAMA, Katsuhiko KITAMOTO(Dept. of Biotechnol., Univ. of Tokyo)

P-30
Պё A. oryzae SǇƐЩǇȢɐR29fʸȾ͹̅ԅӐӟêǇSԿΑͲSĂӑňˌͼÂŉ̑ՕӶ ӹˇՕÃǵ͒ºՕŏˀŌV;Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓՊё Aspergillus oryzae R2/MʸȾÀáTΑѷ=gM/Q/4Օ˗RcJM·QfɶűƣӟêǇ MAT1-1.f/T MAT1-2 jaK;O3dՕ µ²yQʸȾ͹̅jѦ0ūЫȾ4ίƅ=gM/f 1)%ßSϩͪёNSΧσ3dՕA. oryzae Tё˘ħRǇƐˌՕǇƐՕǇƐЩǇjȢɐAf;ORceՕʸȾ͹̅jѦ0OÏɇ
=gf%ɑ&SâļSΧσNՕё˘ȢɐjɛĸAfҸĩƔǇ EcdR S˸ɽRceё˘ȢɐjĂӑ?Օ=dRՕ
Ӯ̋SʸȾ͹̅SÄѵĸȯƔǇ Ime2p OΜųȾjaK AoIme2 SԿΑͲRceՕё˘ħSǇƐˌSȢɐjĂӑAf;ORɐń?G%?3?ՕǇƐSħӧRȢɐ=gGǇƐЩǇ˭SˬӏTǩ=/aS4ƹ7ՕʸȾ͹̅
4¾ǎģN.f;O4ίƅ=gG%ÜƓTՕßSʸȾ͹̅ԅӐӟêǇjԿΑͲAf;ORceՕA. oryzae NSǇƐЩǇȢɐSĂӑňˌj˧҂Af;OjΚΕO?G%
A. oryzae S ecdR ӟêǇ4ΩƳ=gG˗R2/MՕӄЌSϩͪёNʸȾ͹̅jĂӑAfӟêǇ laeAnsdD
 A. oryzae R29fΜųӟêǇSԿΑͲ˗jöѱ?G%;gdS˗jͻ/M·QfɶűƣP0?NǣǹƧԸjѦ/Օ}µ¹Sư΂ЉNёϩѤű?MȢɐ=gfё˘SħӧˬӏjѼǡ?G%ESϹˌՕecdR ΩƳ˗R
29f laeA 2cW nsdD ӟêǇSԿΑͲRceՕё˘ħSǇƐˌSȢɐňͯ4¼ʢ?G%=dRՕǇƐЩǇ
˭SˬӏRK/MTՕӄЌSϩͪёSǇƐЩǇOų˭Sƺ5=SaS4Ѽǡ=gfc0RQJG%ͲƞՕǇ
ƐЩǇ˭ˬӏj¦oyµ¦­´¹¹RceŘԝ?ՕǨĢ?GӟêǇ¦¹u¹jғZf;ORceՕʸȾ͹̅4ѦigM/f3P03SѾˊjѦJM/f%
1) Wada et al. (2011) Appl. Environ. Microbiol. 78; 2819-2829.
Promotion of ascospore formation by overexpressing sexual reproduction-related genes in Aspergillus oryzae
Yuki TANAKA, Feng Jie JIN, Jun-ichi MARUYAMA, Katsuhiko KITAMOTO(Dept. of Biotechnol., Univ. of Tokyo) 50 —P-31
Investigation of the mechanism for septal association of Leashin protein in Aspergillus oryzae
Pei HAN, Feng Jie JIN, Jun-ichi MARUYAMA, Katsuhiko KITAMOTO (Dept. of Biotechnol., Univ. of Tokyo)
Woronin body, a Pezizomycotina-specific organelle, is tethered to the septum in normal growth condition, and it
plugs the septal pore in response to cellular wounding, preventing the excessive loss of cytoplasm. Recently, we
identified a Woronin body tethering protein AoLAH in Aspergillus oryzae1). Deletion of the Aolah gene causes thedisappearance of Woronin bodies near the septum. AoLAH is a single polypeptide with 5,727 amino acids; it iscomposed of a conserved N- and C-terminal regions and a long non-conserved middle region. We found that AoLAH
N-terminal and C-terminal regions function for Woronin body association and tethering to the septum, respectively.
AoLAH C-terminal region fused with EGFP was closely associated with the septum, and its deletion led to the failureof Woronin body tethering to the septum. However, how the AoLAH C-terminal region associates specifically with theseptum is not known. The aim of this study is to investigate the mechanism for septal association of AoLAH. Deletion
analysis of the AoLAH C-terminal region was performed to identify a part responsible for the septal association.
AoLAH C-terminal region consists of approximately 1,000 amino acids. According to secondary structure prediction
analysis, the former 500 amino acids of this region is mostly disordered while in the latter 500 amino acids several
secondary structures such as α-helix and β-sheet were predicted. This structure prediction is similar to those of the
C-terminal region of LAH proteins from other Aspergillus species. Based on these data, deletion of the AoLAH
C-terminal region is being done to observe the effect on the septal association of AoLAH, and complementation
analysis of the deletion fragment for Woronin body tethering will be performed.
1) Han et al. (2014) Eukaryot. Cell 13: 866-77.

P-32 (O-14)
Պё A. oryzae R29fĞýǉȾSİ͹ǇȢɐɛĸ©u¨RԅAfѾˊ
Helge M. DietrichՕͼÂŉ̑ՕӶ ӹˇՕÃǵ͒ºՕŏˀŌV;Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓՊё Aspergillus oryzae R29fİ͹ǇȢɐTՕοՊӏebё˗S˦ё¸ĄǉQPSͺ˩ΕĶͻRȦԪAf
ӳѵQӖνN.f%ɑ&TâļՕĞRcJM A. oryzae Sİ͹ǇȢɐ4ɛĸ=gf;OjƬź?G 1)%ºʘNՕ
Aspergillus nidulans QPNƬź=gM/fc0RՕĞ4´OQJMİ͹ǇȢɐ4Ăӑ=gfS4ºоΕ
N.fOЛ1dgf4ՕA. oryzae SȺϓT;gOT˽ŤǣN.f%A. oryzae 4Ǚ΅Ŏ=gfԕRՕʲ/ǱħSοՊӏeNİ͹Ǉjƹ7ȢɐAf˗4Ӟɟ=gM5GūЫȾ4Л1dgf4ՕESİǇ©u¨T¾ʣ
N.JG%ÜƓTՕ͠ǤAfĞŞԁjӞɟN5f LED Ğ͈jùͻAf;ORceՕA. oryzae 4ĞRȺϓ?
Mİ͹ǇȢɐjɛĸAf©u¨Rԅ?MѾˊjѦJG%ԢсĞ2cWүсĞ͠Ǥ˅åN A. oryzae RIB40 ˗SƧԸjѦ/Օİ͹ǇSȢɐňͯRK/MғZG%ESϹˌՕԢсĞ͠ǤRcfİ͹ǇȢɐSɛĸ4ѷdgG4ՕүсĞNTĞSȦԪTѼǡ=gQ3JG%;S;O3dՕĞRcfİ͹ǇȢɐSɛĸTԢсĞRýǉAf;O4ί=gG%;SĞȺϓS©u¨jѾˊA
fG`ՕA. oryzae |¨¹¡¹ceՕA. nidulans SԢсĞŧǚó LreA OүсĞŧǚó FphA RΜųQ·yҮj}¹AfӟêǇjѷ/H?ՕEgFg AolreAՕAofphA OžŴ?G%ӟêǇΩƳ˗jöѱ?GϹˌՕAolreA ΩƳ˗R2/MԢсĞRcfİ͹ǇȢɐSɛĸ4ѷdgQ7QJG%ºʘNՕAofphA ΩƳ˗NTՕӴ͹ƣ˗Oų˭RԢсĞRceİ͹ǇȢɐ4ɛĸ=gG%?G4JMՕA. nidulans S LreA O FphA TĞ
RȺϓ?ՕŖғ?Mİ͹ǇȢɐjĂӑAfSRǣ? 2)ՕA. oryzae NT AoLreA S^4ĞýǉΕRİ͹ǇȢɐjɛĸ?ՕAoFphA T;SӖνRԅ¿?Q/;O4ʣd3RQJG%
1) Hatakeyama et al. (2007) Biosci. Biotechnol. Biochem. 71:1844-9. 2) Purschwitz et al. (2008) Curr. Biol. 18:255-9.
Investigation of light-dependent repression of conidiation in Aspergillus oryzae
Helge M. DIETRICH, Yuki TANAKA, Feng Jie JIN, Jun-ichi MARUYAMA, Katsuhiko KITAMOTO(Dept. of Biotechnol., Univ. of Tokyo)

 51 —P-33 (O-15)
u¹¤·u¤±oɛĸĸȯƔǇ CreA ṰȾŎ˅åR2/MǍǓŎAf
ͼÂͷȃՕʗҝǫȜՕÓżŌËՒˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓ ϩͪёSu¹¤·u¤±oɛĸT, C2H2 ƣҸĩƔǇ CreA RcJMĸȯ=gf;O4΢dgM/f%
Aspergillus nidulans NT, u¹¤·u¤±oɛĸRԅifßSƔǇO?M®w·ŎbЯ®w·ŎRԅ¿AfƔǇ4ųǓ=gM2e, ;gd4 CreA SİѾRԅ¿AfūЫȾ4ɫʀ=gM/f%?3?,
CreA SǍǓȾRK/MT[OkP΢ѷ4Q/%ˀΧσNT, m§·̼ŅRceΑͲɛĸūЫQ thiA µª¹¹ĸȯ½N 3FLAG zѤű CreA jՊёNΑͲ=C, ˭&Q͙ϰ͈ǉƞ½R29f CreA SǍǓȾjѾˊ?G% ļƧԸ?G 3FLAG zѤű CreA ΑͲ˗Sёójm§·̼ŅƧƠRλ?MΑͲjɛĸ=CGȫ, Űο͙ϰ͈j̼Ņ?, ϸʪΕR CreA ·yҮӵjғZG%ESϹˌ, ͙ϰ͈jŅ1Q/ƭűb¦³¹, ³y¹, wµ¹, z² µ¹³j̼Ņ?GƭűRT CreA TȽӎRİѾ=gG%ºʘ, z³}¹b¦·¹j̼Ņ?GƭűRT CreA 4ј?7ǍǓŎ?G%Űο͙ϰ͈Su¹¤·u¤±oɛĸYSԅ¿jғZfG`, ··ƧƠRŰο͙ϰ͈j̻ű?, µ¹ȢɐЫj̎Һ?G%ESϹˌ, z³}¹O¦·¹j̼Ņ?GƭűRӴ͹˗Sµ¹ȢɐЫ4 creA ΩƳ˗O̎Һ?Mј?7ɛĸ=gG%â¼SϹˌ3d, CreA Tu¹¤·u¤±oҎǨ˅åR2/MǍǓŎ=gf;O4ίƅ=gG%Ͳƞ, CreA SϳЩħǯƞb®w·¸Я®w·ŎԅӐƔǇS CreA ǍǓȾYSԅ¿RK/MѾˊjѦJM/f%ˀΧσT'Ӏˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%
Stabilization of carbon catabolite repression regulator CreA under the activation condition in Aspergillus oryzae.
Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi
(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ.)

P-34
ՊёR29ft¹l¹Rcf˘SİѾՒy´tl¹ՓS҈þ̥»ҝԒǐՕѐԄԒȹՕŏˀŌV;Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓ)ΚΕ*t¹l¹Tt¹l~¹¨RcJMϳЩҮɐİjƗ/Ӄ^Օ̶Щ/²¹¨NİѾAfӖνN.eՕΟ˘͹ͧRȎ7Ąǉ=gM/f%Պё Aspergillus oryzae T˘ģójt¹l~¹¨NŦeƗ^Օ̶ЩYҾӉ?İѾAf;O4΢dgM/fՒy´tl¹Փ
%;gTՊё4ƹ˘͹ͧN.fG`RūЫQͲҠN.f%?3?ՕESİǇ˶ˬb͹ʹǋΕɈЗSҋϳT¾ʣN.f%ˀΧσNTՕA. oryzae 4y´tl¹jҎǨAf˅å¸˶ˬSѾʣjΚΕO?MՕy´tl¹S҈þʘ̥S
έχjΚɫ?G%)ʘ̥¸Ϲˌ*GFP Ѥű·yҮ4t¹l¹RcJM̶ЩRŦeӃ]gfOՕ·yҮİѾӮϰRceİѾ=gՕGFP S^4̄ǉAf%;S GFP S·jpq·µ̥N˧įAf;ONՕt¹l¹RcfΚΕ·yҮSŦeӃ^j҈þAfʘ̥4Ӯ̋QPNƹ7ͻ/dgfՒCleavage
assayՓ%˘ҮRǯƞAf· H2B Rǣ?M Cleavage assay jѦJGO;hՕƧԸʪԄSϸӖRëJM˧į=gf EGFP ӵ4ƱŅ?G%]GՕѣĞԱȲӿNѼǡ=gG̶ЩħS EGFP ѣĞaų˭Sĕŵjί?
G%ͲƞՕt¹l¹˸ɽ˗Aoatg8 ˗R2/M Cleavage assay jѦ/ՕEGFP S·S˧į4t¹
l¹ýǉΕN.f;Ojέҍ?M/f%;S҈þ̥jͻ/MŰοS˖Ը˸È˅åRK/M˧҂?GO;hՕ͙ϰ͈¸φϰ͈ԴԹR2/My´tl¹4ҎǨ=gf4Օ²·ӯՕu²p¨Օ¦zp¨S˸ÈNTҎǨ=gQ/;O4ί=gG%

Evaluation of nucleophagy, degradation of nucleus by autophagy, in Aspergillus oryzae
Takahiro MITANI,Takashi KIKUMA,Katsuhiko KITAMOTO(Dept. of Biotechnol., Univ. of Tokyo) 52 —P-35
ՊёR29f Acyl-CoA binding protein (AoAcb1, AoAcb2)Rcfͨ̃İ̤ϸҴSѾˊǿũнȋՕѐԄԒȹՕŏˀŌV; Ւˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՓǩЩó~³ójϸͽ?Q/ͨ̃Qİ̤ϸҴRcf·yҮİ̤SºKO?MՕӮ̋R2/MՕ
Acyl-CoA-binding protein (Acb1)SϳЩƸYSİ̤4Ƭź=gM/f%Acb1 Tİ̤z³өĲjɪGQ/·yҮN.f4Օ˖ԸԴԹ˅åNϳЩƸYİ̤=gf%ESİ̤˶ˬRTt¹l¹ԅӐ·yҮ
QPS·yҮ4ȷѵO=gf%Ӯ̋NTͨ̃İ̤ϸҴSΧσ4ѦigM/f4ՕϩͪёR2/MT[OkPƬź4Q/%]GՕӮ̋QPNT ACBP (Acyl-CoA Binding Protein)ª¹jʸAf·yҮT 1 KH
9N.f4ՕϩͪёSƹ7NT ACBP ª¹jɪK·yҮ4 2 KǉƞAf%E;NˀΧσNTՕA. oryzae
4ʸAf 2 KS Acyl-CoA-binding protein S˶Ыjʣd3RAfOOaRՕϩͪёR29fͨ̃İ̤ϸҴjΑ
ѷAf;OjΚΕO?G%
S. cerevisiae S Acb1 S£ªµzӟêǇ Aoacb1 O Aoacb2 TEgFg 365 m§ӯՕ143 m§ӯj}¹
?M/f%;g]NSǯƞѼǡRceɑ&TՕAoAcb1 4ϳЩħNͪˬӏjȢɐ?MȲǩϗýǉΕRλŊAf;OՕAoAcb2 4Ӯ̋ Acb1 Oų˭RϳЩҮÂRɧʌAf;Ojί?G%AoAcb1 4ʸAf ACBP ª¹
O TraP ª¹jEgFg˸ɽ=CG AoAcb1 R EGFP jѤű=CMѼǡ?GO;hՕACBP ª¹˸
ɽ AoAcb1 TͪˬӏSλŊ4ұ;dQ7QeՕTraP ª¹˸ɽ AoAcb1 TϳЩҮÂRɧʌ?M/G%ӍȉSʘ̥NT Aoacb2 ΩƳ˗jȮf;O4N5Q3JGG`ՕthiA µª¹¹ĸȯ½N Aoacb2 jΑͲ=CՕƧƠÂRm§·j̼Ņ?MΑͲjɛĸ?GO;hՕAoacb2 ˅åΑͲ˗O Aoacb1 ΩƳ Aoacb2 ˅åΑͲ
˗R2/MՕųνȑS}µ¹ŔȨŚǪ4Ѽǡ=gG%]GՕpr·µ̥RceՕHA zjѤű=CG AoAcb2 4ƧԸ¼̽R˧į=gG%ͲƞՕ;SϹˌ4͋ёRcf·yҮS͋įNQ/;OjέҍAfOOaRՕAoAcb1 RK/MaϳЩƸYİ̤=gM/f3P03j˧҂ÂN.f%
Analysis of unconventional secretion pathway of acyl-CoA binding proteins (AoAcb1, AoAcb2) in A. oryzae
Kouhei KAWAGUCHI, Takashi KIKUMA, Katsuhiko KITAMOTO(Dept. of Biotechnol., Univ. of Tokyo)

P-36
Պё Aspergillus oryzae S¥²²·ӯáҚԅӐӟêǇS˶ЫѾˊƹͼ ń͹, ƺũ V3f, ˨ˀ ɏºՒӀΧ˶ˬ ԳІΧՓ
 ¥²²·ӯTՕʎĈ3dʎΔĈS²·ӯՒt³²·ӯՓ4Կr³x¹²·ӯϹű?GΛӾͪS¥²¦¹
N.eՕy²m3dƄÌԲ]NS͹ͧSϳЩRȎ7ǉƞ?M/f%ϳЩħR29f²·ӯOr³x¹
SҦќOғϙ4ESÄѵQȧŀN.fO=gM/f4ՕՊё Aspergillus oryzae R29f¥²²·ӯSҋϳQ
˶ЫRK/MTʣd3R=gM/Q/%ɑ&TՕӳӶǳ´ՕšWӯŎ´ǉƞ½R2/M A. oryzaeS¥²²·ӯњςӵ4ƺ57ƷŊAf;Ojʣd3R?ՕʨȌȑƬź?G%ÜƓɑ&TՕ¥²²·ӯáҚԅӐӟêǇSΩƳ˗jöɐ?ՕESѾˊjѦJG%Ӯ̋ Saccharomyces cerevisiaeS¥²²·ӯ¥²©±¹ՒVtc1ՕVtc2ՕVtc3ՕVtc4ՓՕr·¥²£l¹ՒPpn1ՓՕrw¥²£
l¹ՒPpx1ՓSt³µzj}¹AfӟêǇjՊё|¨¹¡¹ceѷį?ՕEgFg vtcAՕ
vtcBՕvtcDՕppnAՕppxA O?ՕΩƳ˗jöɐ?G%ŰΩƳ˗TՕ}·µ¹³˗O̎Һ?MՕ¥²²·ӯSњςӵRƷŎTѷdgGaSSՕёϩɐԁՕİ͹ǇȢɐRƺ5QƷŎTѷdgQ3JG%ͲƞՕӳӶǳ´ՕӯŎ´ǉƞ½R29fŰΩƳ˗SѫͲƣRK/MѾˊÂN.f%ˀΧσSºӧTՕʜˀǋѧɯкéθǋΧσҨņɐÐ˩Sņɐjŧ9MѦigGaSN.f%

Functional analysis of polyphosphate related genes in Aspergillus oryzae
Sawaki Tada, Hikaru Ohkuchi, Ken-Ichi Kusumoto (NFRI, NARO) 53 —P-37 (O-11)
Maintenance of active directional growth by perpetual assembly and disassembly of polarity
sites
Norio Takeshita1,4 Yuji Ishitsuka2, Natasha Savage3, Yiming Li2, Anna Bergs1, Daria Kohler2, Rebecca Donnelly3, G.
Ulrich Nienhaus2, Reinhard Fischer1Ւ1Dept. of Microbiology, Inst. for Applied Bioscience, 2Inst. for Applied Physics,
Karlsruhe Institute of Technology (KIT). 3Dept. of Functional and Comparative Genomics, Inst. of Integrative Biology,
Univ. of Liverpool. 4Univ. of Tsukuba, Faculty of Life and Environmental Sciences.)
Polar cell extension depends on spatially very defined insertion of new membrane. In filamentous fungi, like
Aspergillus nidulans hyphal tips (3 µm in diameter) extend with speeds of 0.3 – 1.0 µm per min, which means anincrease of the membrane surface of 0.9π – 3π µm2 per min. Given that secretory vesicles are about 40 nm in diameter,
massive exocytosis of about 600 – 2000 vesicles per min is required to ensure sufficient membrane supply even in thecase that endocytosis is ignored. On the other hand, secretion at the hyphal tip depends on the exact positioning of
landmark or cell-end marker proteins, anchored in the membrane. The active exocytosis in filamentous fungi has apotential to diffuse membrane associated polarity markers but they can maintain the polarity to form hyphae. Here, we
discovered a mechanism how polar growth can be maintained despite the continuous, massive disturbance of cell-end
marker positioning caused by membrane insertion. In A. nidulans the cell-end marker protein TeaR reaches the tip
through microtubule- and actin-dependent transport. Once at the tip, TeaR recruits other proteins among which is theactin forming formin SepA. Thus the actin cytoskeleton assembles at the site of TeaR, and delivers more TeaR to thissite. This positive feedback loop causes increased secretion, local membrane extension, but also dilution of the cell-end
markers. To solve the contradiction, the polarity is reconstructed by microtubules repeatedly in addition the cell growth,
membrane extension, occurs in a fluctuation manner. The localization and dynamic behavior of TeaR is investigated bysuper-resolution microscopy technique PALM (photoactivation localization microscopy).

P-38 (O-12)İ̤Ӯϰ͹ͺRԅ¿Af Aspergillus nidulans SunA S˶ЫѾˊпǵ.B^ՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ¸͹žӀǋՓ)ΚΕ* AHP1102 Tm§±¹Օ ³±¹Օµm¹QPİ̤ӮϰS͹ͺȾ4ŵ¼?GƷ·˗N.e sunA ӟêǇTˀƷ·jΜѰAf%A. fumigatus R2/M SunA St³µz Sun1 TϳЩƲ β-1, 3-glucan
RöͻAfӮϰN.f;O4ӄȌί=gM/f%ˀΧσNT SunA S˶ЫՕE?Mİ̤Ӯϰ͹ͺȾR¿1f
ȦԪjѾˊ?G%)ʘ̥¸Ϲˌ* ]B AHP1102 R29f sunA ӟêǇ¼SƷ·jųǓ?G%ESϹˌՕ;SƷ·Tyµª
¹¨ I S sunA Sµª¹¹ԮƦOyµª¹¨ VIII S AN0430 ˬӏӟêǇħOSϷ^ɺ1Rce͹@G;O4ʣd3OQJG%SunA 4İ̤Ӯϰ͹ͺȾRȦԪj¿1f;OjέҍAfG`ՕΩƳ˗ՕԿΑͲ˗jöѱ?G%ΩƳ˗NT AHP1102 Oų˭Rİ̤ӮϰS͹ͺȾŵ¼4^dgG4ՕԿΑͲ˗NTʸɈQȦԪTѷdgQ3JG%]GՕёóƸ·yҮj SDS-PAGE N̎ҺAfOՕΩƳ˗NTӴȾ˗R̎Zƹ˭Q·yҮ4ёóƸRǉƞAf;O4ʣd3OQJG%SunA 4ϳЩȢɋR¿1fȦԪjԱȲӿѼǡ?GO;hՕΩƳ˗NTёϩSȢͪ4/WKRQfQPS·ȉ4^dgG%ʳRTϳЩƲRöͻAfŎǋͧҮN.f
Calucofluor white, Congo red QPRǣAfΩƳ˗SɊŧȾjӴȾ˗O̎Һ?GO;hՕΩƳ˗NTɊŧȾjί
?G%;gdS;O3d SunA SϳЩƲűɐ¸İѾYSԅ¿4ίƅ=gG%ºʘNϳЩƲSȿȉȾRԅ¿A
fҸĩƔǇՕɆƬêӘƔǇO sunA ӟêǇΑͲOSԅāj˧҂?G4ՕnikA, mpkA, rlmA /BgSΩƳa sunASΑͲRȦԪj¿1Q3JG%Functional analysis of Aspergillus nidulans SunA involved in extracellular enzymes production
Azumi Funayama, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi(Graduate Sch. of Bioagric. Sci., Nagoya Univ.) 54 —P-39
Aspergillus nidulans R29fµo·w¹ C Rcfu³p¨Ⱥϓz³êӘϸҴĸȯ˶ˬSѾˊͤǵͶË 1Օȹ̧ę 2ՕŲǿřʑ 3ՕƩħѯÇ 1 Ւ1 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹ȀՕ2 ǸɗŐƺ¸/iMˈŏ©nu³¸©v·y˶ˬՕ3 ˈӀƺ¸Ⱥ͹θ¸otՓ Aspergillus nidulans Sµo·w¹ C N.f PkcA T͹ХRȷԭN.eՕϳЩƲSǎģȾЂɪՕ˪Ⱦ͹ԁՕÑ˹áҚͺͧS͹ͺĸȯQP˭&QͲҠRԅ¿Af;O4ίƅ=gM/f4ՕES˶ЫSҋϳRK/
MTʾѾʣQӧİ4ƹ/%ȡΧσz³¹NT pkcA ̈́ȑɊŧȾ˗jͻ/G PkcA ƿ̭˅åR29fЃДΕҸĩѾˊjѦQJM2eՕESϹˌ;S˅åNTϳЩħ Ca2+͕ȑSȿȉȾЂɪRԅifӟêǇS mRNA 4ƱŅ
Af;O4ʣd3OQJG%ϳЩħ Ca2+͕ȑSȿȉȾЂɪRTu³p¨Ⱥϓz³êӘϸҴ4ӳѵQȧŀjɣ04Օ;SϸҴSҸĩƔǇN.f CrzA ýǉΕRҎǨ=gf;O4΢dgM/f 25 ӟêǇS0IՕ[OkPSӟêǇS mRNA 4 PkcA ƿ̭˅åNƱŅ?M/G%=dR crzA ˸ƿ˗jͻ/GǓӵ PCR ̥Rcf
ҸĩѾˊ3dՕPkcA ƿ̭˅åNS;gdSӟêǇS mRNA ӵSƱŅ4ӧİΕR CrzA RýǉAf;O4ίƅ=gG%CrzA T Ca2+RȺϓ?MϳЩҮ3d˘RλѦ?ՕӟêǇSҸĩjҎǨAf4ՕPkcA ƿ̭˅åNT C
ʿϊR EGFP jàŅ?G CrzA S˘RǯƞAfŀű4ƱŅ?M/G%;gdS;O3dՕPkcA 4Կ̈́´˅å½Nu³p¨Ⱥϓz³êӘϸҴjҡRĸȯAfūЫȾ4Л1dgG%ͲƞՕPkcA S½̮N˶ЫAf MAP w¹N.f MpkA Su³p¨Ⱥϓz³êӘϸҴSĸȯYSǜ¿RK/M˧҂ÂN.f%Regulation of Ca2+ signaling pathway by protein kinase C in Aspergillus nidulans
Takuya Katayama1, Yu Shiwa2, Hirofumi Yoshikawa3, Hiroyuki Horiuchi1 (1Dept. of Biotechnol., Univ. of Tokyo,
2

Iwate Tohoku Medical Megabank Organization, Iwate Medical Univ., 3Dept. of Biosci., Tokyo Univ. of Agric.)

P-40 (O-13)ϩͪё§}·²mS˶ЫYS·w¹ HysA Sԅ¿ˋʟϫՕǩǺɏÝՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽՒŴƺԍ¸͹žӀՓϩͪёS͸ưȺϓRTՕ͹ͧRȎ7Ąǉ=gG His-Asp ²·ӯ²´¹ɆƬêӘ˶ˬ4ӳѵQȧŀjɣJM/f;O4΢dgM/f%;S¨NTՕ͸ư ·¹N.f·w¹ՒHKՓ3dS²·ӯƨҸλRcJMɆƬ4ϳЩħRêӘ=gf%âļigigTՕª³ϩͪё Aspergillus nidulans S HK ΩƳ˗Ւ13 οԲՓR29f̭ȾӯϰοՒROSՓSΑ͹jѼǡ?ՕHysA SΩƳ˗R2/M ROS SΑ͹´¡³4Կ
/;Ojѷ/H?G%ӯϰŽŷjѦ0͹ͧNTՕ§}·²mSԠǇêӘϪN ROS 4Α͹Af;O4΢dgM/f%§}·
²m4˽ȉQԕRT ROS j̍͜ŎAf;O4ūЫH4Օ§}·²m4˶Ыjƿ0OΑ͹?G ROS 4ϳЩħRњς?Օ·yҮb DNA R©¹j¿1f%hysA ΩƳ˗R2/MΑ͹?G ROS TՕ§}·
²m˶ЫSƷŎRcJMΑ͹њς?GūЫȾ4Л1dgG%E;NՕhysA ΩƳ˗j 3 ʜԄƧԸ?ՕгԠîS͹@G̭ȾŎ§}·²mj˧įAfѣĞсϰՕMito Tracker Red Nˑс?ՕԱȲӿ½NѼǡ?G%ESϹˌՕΩƳ˗NTՕ̭ȾŎ§}·²m4İ͹ǇːR2/MčJMǯƞ?M/G%ROS SΑ͹Tİ͹Ǉː
R2/MʶaȠ7Ѽǡ=gf;O3dՕ;Sče4 ROS Α͹SŞƔN.f;O4Л1dgG%ˀΧσNTՕЇсѣĞ·yҮ GFP jͻ/G HysA SǯƞѾˊSϹˌaøCՕɆƬêӘƔǇN.f HysA 4PSc0R
ϩͪё§}·²mS˶ЫRԅ¿Af3ЛǡAf%
Possible involvement of Histidine kinase HysA in mitochondrial function of Aspergillus nidulans
Saki Hayashi, Kensuke Kojima, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi(Graduate Sch. of Bioagric. Sci., Nagoya univ. ) 55 —P-41
ϩͪё Aspergillus nidulans R29f²·ӯƨäÝƔǇ YpdA O´¥·´x­´¹
¹SskAՕSrrA SΜÒöͻSѾˊδԄ̩Ç 1ՕЇǿѯр 1ՕѕŞƺα 2,3ՕŪǿďƼӦ 4ՕÂǵΟͽЕ 2ՕŲѷƉ 2ՕԊӧʍɄ 1,2
Ւ1 ˈŏƺԍ¸͹ͧͺ˩ŁɐՕ2 ˈŏƺ¸ʾˆΧՕՒͲՓ3 Œїƺ¸Οё·¹Օ4 °¹¤²ƺՓ

 His-Asp ²·ӯ²´¹ɆƬêӘϸҴTy²m3dԿϑ˦ͧRиf]NȎ7Ąǉ=gGʬӕΕQ͸ưȺϓ˶ˬN.f%ϩͪёRaˀϸҴTĄǉ=gM/f4ՕˀϸҴSˬɐѵϰN.f²·ӯƨäÝƔǇՒHPtՓS˶ЫRK/MT¾ʣQ͚4ƹ/%ª³ϩͪё Aspergillus nidulans R2/MՕHPt j}¹Af ypdA ӟêǇ
S˸ɽTй́N.f;O4ӟêǋΕR҇ʣ=gM/faSSՕ˸ɽ4й́OQfѵƔSͨǓRTиJM/Q/%]GՕ´¥·´x­´¹¹ՒRRՓN.f SskAՕSrrA OSΜÒöͻRK/MaҋϳQɆƬTȮd
gM/Q/%E;N͐МdTՕypdA ӟêǇSΑͲjĸȯūЫQ Conditional-ypdA ˗ՒCypdA ˗Փ2cW CypdA
˗jѻ˗O?G RR ΩƳ˗ՒCypdA-sskAΔ,CypdA-srrAΔ, CypdA-sskAΔsrrAΔՓjӏɐ?ՕHPt O RR SԅāRK/MѾˊjӑ`M5G%
 ÜƓՕalcA µª¹¹Rcf ypdA SΑͲĸȯjʶӜŎ?ՕΑͲɛĸ˅åNSѫͲƣjѾˊ?GSNՕESϹˌRK/MƬźAf%]BՕļƧԸʪR CDTFYՒCDՔ´t·, ³y¹ՕӮ̋rwՓƧƠj
ͻ/f;ONՕǍǓ?G ypdA SǓȉΑͲͪɋ4ǕͲAf;O4ʣd3RQJG%]GՕˀ˅åNƧԸ?GёójΑͲɛĸƧƠRλ?GO;hՕŰ CypdA Ʒ·˗Oa ypdA SҸĩӵ4Ӵ͹˗S 10 İS 1 νȑRï½?Օ
ypdA SҸĩӵƷŎRë0½̮ӟêǇSȺϓaѼǡ=gG%ͲƞՕWestern ѾˊRce YpdA ·yҮSΑͲӵjѾˊAfOOaRՕYpdA ΑͲƷŊRë0͹ХɅŎՕёϩȢɋS·ȉRK/MѾˊjӑ`M/f%ՒˀΧσTՕӀˋ̒ͺ˩¸Գƀͺ˩θǋəѧɷӑÐ˩Sʆɼjŧ9MѦigGaSN.f%Փ
Analysis of the relationship between the histidine-containing phosphotransfer protein,YpdA, and the response
regulators, SskA and SrrA, in Aspergillus nidulans.
Yasuyuki Fukuma, 1Yura Midorikawa, 2,3Daisuke Hagiwara, 4Kentaro Furukawa, 2 Mayumi Nakayama, 2Akira

1

Yoshimi, 1,2Keietsu Abe(1Grad. Sch. Agric. Sci., 2NICHe, Tohoku Univ.,3 MMRC, Chiba Univ. 4 Göteborg Univ)

P-42
ϩͪё PKC Rͨ·ΕQʗѸԉǘľRǣAfӮ̋y²¹·zϪSʶӜŎȏůӥƾ 1ՕÂǵΟͽЕ 2ՕŲѷƉ 2ՕѠǷʰĻ 3Օ̞ű̽ 3ՕƩħѯÇ 4, ˡǵεʣ 5, ԊӧʍɄ 1,2
Ւ1 ˈŏƺԍӀ¸͹ͧͺ˩Łɐ, 2 ˈŏƺ¸ʾˆΧՕ3 y§moŎǋȀ˩, 4 ˈƺԍӀ, 6 ÂƾƺʹȀՓϳЩƲˬϚz³êӘϸҴTՕΟёSϳЩƲˬϚR2/MӳѵQȧŀjɣJM/f%ˀϸҴjˬɐAf·yҮS0Iµo·w¹ CՒPKCՓTՕͨRÂȶΕQȧŀjˌG?M2eՕϩͪёSª³͹
ͧ Aspergillus nidulans S PKCՒAnPkcAՓbo/aIΎёS PKCՒMgPkc1ՓS˸ɽTй́N.f;O4΢
dgM/f%;S;O3dΟёS PKC TʗGQɝΟёľS˰ΕO?M̨Κ=gM/f%;g]NRɑ&TՕMgPkc1 SԉǘľɵϱjΚΕRՕχóˬӏª²·zRcfo·²}y²¹·zjѦJM5G%ESϹˌՕʎοSԉǘľĊѰŎűͧ4ѷį=gՕǟƻƧƠ¼NS͹Хԉǘ҉Խ3dՕMgPkc1
ԉǘľO?M Z-705 4Ӟɞ=gG%ºʘՕˀŎűͧToї¼NSџľ҉ԽR2/MԱјQňˌTҍ`dg
BՕŎűͧʇƷRcf̭Ⱦŵ¼4Ғ԰OQJM/f%E;NˀΧσNTՕZ-705 SʇƷjѷɳ1ՕZ-705 2c
WESԲЌŎűͧS̭Ⱦj҈þAfӮ̋y²¹·zϪSԃΑjӑ`M5G%ˀ҈þϪTӮ̋ Pkc1 Sw
¹©o·jϩͪёͽˆSaSRГɺ?GՕӮ̋ϩͪёw©± PKC ΑͲ˗jͻ/M2eϩͪё PKC
ԉǘľɵϱRʸňN.f;O4ίƅ=gM/f%ÜƓ=dR̭Ⱦ҈þSϦȑŵ¼jҁfG`͙ϰ͈bƧԸ̈́ȑQPSƧԸ˅åj˧҂?G%ESϹˌʶǪƧƠR2/Mv±y¹j͙ϰ͈RAf;ONw©±
PKC ΑͲ˗S Z-705 RǣAfɊŧȾj˽έ3KĨͲc7҈þAf;O4ūЫOQJG%Ͳƞ Z-705 ǉƞ½
NSӮ̋SȢɋѼǡb}µ¹Ȣɐ҉ԽRceˀџľSёóYSöͻjceҋϳRѾˊ?M/f%
Improvement of the yeast-screening system for novel specific inhibitor of protein kinase C of filamentous fungi
Fumio Shoji1, Mayumi Nakayama2, Akira Yoshimi2, Tomonori Fujioka3, Kiyoshi Kawai3, Hiroyuki Horiuchi4, Hideaki
Umeyama5, Keietsu Abe1,2 (1Grad. Sch. Argric. Sci. & 2NICHe. Tohoku Univ., 3Kumiai Chemical Industry Co., Ltd., 4
Grad. Sch. Agric. Sci. Tokyo Univ., 5Facul. Sci. Engin. Chuo Univ.) 56 —P-43
Aspergillus nidulans S wspA S˶ЫOw·űɐӮϰǯƞŎR29fȧŀo µՕʥ ̱жՕƩħ ѯÇ Ւˈƺԍ¸Ӏ͹θՓ
糸状菌の菌糸先端生長において，エンドサイトーシスにより取り込まれたタンパク質が再度先端に輸送されるリサイクリング機構が重要であることが示唆されている。一方，演者らのグループでは Aspergillus
nidulans を用いて，菌糸先端生長に重要な働きを持つキチン合成酵素 ChsB，ミオシン様タンパク質融合型キチン合成酵素 CsmA が菌糸先端に局在することを示している。今回，酵母 Saccharomyces cerevisiae のオルソログなどでエンドサイトーシスへの関与が示唆されている A. nidulans の遺伝子 wspA について，その機能解
析とキチン合成酵素の菌糸先端への局在における役割について解析した。その結果，wspA 破壊は野生型遺伝

子とのヘテロカリオン株としてのみ取得でき，wspA が破壊された遺伝子のみをもつ分生子は発芽時に無方向性の生長をするだけで発芽管を形成せずに生長を停止した。これらのことから wspA は生育に必須の遺伝子で分生子発芽時の極性の確立に必須の機能を持つことが示された。さらに wspA の発現を制御できる株において，wspA の発現を抑えたところエンドサイトーシスが阻害されたことから wspA が菌糸におけるエンドサイトー
シスに重要な機能を持つことが明らかとなった。一方 wspA の発現を抑えた株ではキチン合成酵素 CsmA の菌糸先端への局在パターンに変化が見られたことから，CsmA の菌糸先端への局在において重要な役割を持
つことも示された。現在，ChsB の菌糸先端への局在における wspA の関与について検討中である。

Functions of wspA of Aspergillus nidulans and its role in the localization of chitin synthases
Lu Zheng, Hiro-omi Hoshi, and Hiroyuki Horiuchi (Dept. of Biotechnol., Univ. of Tokyo)

P-44
Պё Aspergillus oryzae admA, admB ӟêǇ˸ɽ˗SϳЩƲˬɐƹϧO RNA-Seq Ѿˊǩˋɦƍ 1Օļͼ̱ 1ՕŪǼĶϫ 2ՕΥÔºƽ 2Օʸ̖Ń 2Օόħӗԙ 1ՕǵȢ̫ȋ 1
Ւ1 ˈӀȀƺԍ¸Ⱥ͹θՕ2 ˈӀȀƺԍ¸ӀǋϪ|¨Û˃Хɐµz±¨Փ) Ч ʭ 2 c W Κ Ε * admA, admB ӟ ê Ǉ T Օ Պ ё Aspergillus oryzae S ADAM ( A Disintegrin And
Metalloproteinase ) j}¹AfӟêǇN.f%ADAM TՕµm¹©o·Ono·z²·
©o·ՕгҥӍԮƦjɪK·yҮN.eՕƄÌԲR2/MϳЩɶΠb·yҮµ ·zՕz
³êӘQPRԅ¿Af;O4΢dgM/f%;g]NRՕadmAՕadmB ӟêǇSŘͫ2cWÑӳ˸ɽ˗jöѱ?ՕѫͲƣjѼǡ?G%ESϹˌՕ˸ɽ˗T calcofluor white b congo red RɊŧȾjί?Օİ͹ǇѫԦ
Sˬӏ4ƷŎ?M/G;O3dϳЩƲˬӏRƷŎ4͹@M/f;O4ίƅ=gG%ÜƓTՕ˸ɽ˗SϳЩƲ
R͹@GƷŎjceҋϳRғZfG`RϳЩƲˬɐɐİSİ΁2cWϧSǓӵjѦJG%=dRՕƷŎ4͹
@GʹͽjɵfG`ՕRNA-Seq ѾˊjѦJG%)ʘ̥2cWϹˌ*̒͢Om³u²̶͋Rce˸ɽ˗O}·µ¹³˗Sİ͹Ǉ2cWёϩSϳЩƲˬɐɐİjİ΁?ՕȮdgG΁İRK/Mq¹³¸Ϋӯ̥Rcf w¹ŶӵSǓӵՕBlix ̥Rcf w§·ŶӵSǓӵjѦJG%ESϹˌՕŰ˸ɽ˗NTϳЩƲˬɐƹϧ4ӵΕRƷŎ?M2eՕESƷŎ4
˸ɽ˗̌R·Qf;O4ʣd3RQJG%RNA-Seq ѾˊTՕİ͹ǇȢɐ˅åN.f}¨x¦ƙóƧƠN
72 ʪԄƧԸ?GƧԸͧ3dғѱ?G total RNA jͻ/G%ѾˊSϹˌՕϳЩƲˬɐƹϧSӵΕƷŎOΜԅS.fϳЩƲűɐԅӐӟêǇSΑͲƷŊ4ѷdgG%=dRՕw¹ӟêǇbҸĩƔǇӟêǇSÂRaƷŊ
?M/fӟêǇ4ѷdgG%
 Q2$ˀΧσSºӧT͹Χ ·¹ƨήɷӑÐ˩Sº͸O?MѦigGaSN.f
Analysis of polysaccharide composition of cell wall and RNA-Seq in Aspergillus oryzae admA, admB gene deletion strains
Takuji Kobayashi1, Hiroshi Maeda1, Toshinori Kozaki2, Kazuo Ishii2, Tsutomu Arie2, Michio Takeuchi1, Youhei Yamagata1(1Dept. of Applied Life Science, Tokyo Univ. of Agriculture and Technology, 2Tokyo Univ. of Agriculture and Technology) 57 —P-45
Aspergillus nidulans R29fv±y±¹ҸλӮϰS˶ЫѾˊͤ̀ͽ÷Ǉ 1ՕϛƮʟϫ 2Օ̣Ǖ 2Օ̲ӴƟҼ 1Օόǿў 3ՕȫѠ˽Ķ 3ՕӴ˄Ɗȍ 1ՕǷɦÑ 1
Ւ1 ǻƥƺ¸͹ͧ͹žՕ2 Ƿǵƺԍ¸͸ư͹žՕ3 Êƺԍ¸ӀՓϩͪё Aspergillus nidulans R29fv±y±¹ՒGalfՓҸλӮϰ GfsA TՕˀΧσǖRceųǓ=gG%;g]NR GfsA T UDP-Galf jϧü¿óO?M O-z²u·ĆԷ·yҮR Galf jҸλAf̭Ⱦjʸ
Af;O4ʣd3OQJM/f%?3? GfsA SŧǚƨҮbՕűɐ=gf Galf ϧӾSϹűӧî2cWχóөȒTʣd3OQJM/Q/%ˀΧσNTŧǚƨҮO?M pNP--Galf ͻ/G GfsA S̭ȾͅǓϪSԃΑj҉^
G%ϧü¿óO?M UDP-Galf jͻ/ՕϦѱ?G GfsA O 37N 24 ʪԄŤȺ=CՕŤȺͺͧj HPLC Rü¿?GO;hՕŧǚƨҮOT·QfʗѸQ¹y4 2 Kҍ`dgG%E;NȮdgGŰ¹yjİŦ? LC-MS
2 c W LC-MS/MS R c f Ү ӵ İ ˊ j Ѧ J G % E S Ϲ ˌ Օ 2 K S  ¹ y T E g F g UDP-Galf-Galf Օ
UDP-Galf-Galf-Galf SİǇӵOºй?G%â¼S;Oce GfsA T pNP--Galf jŧǚƨҮO?Mҍқ?ՕGalf̄ƨR Galf ̄ƨjǪQ7Oa 2 K]NҸλAf̭ȾjʸAf;O4ʣd3OQJG%ºʘՕGfsA RTm§ӯ´¡³NEgFg 27.5%O 26.0%SΜųȾjʸAf GfsB O GfsC 4ǉƞ?M/f4ՕESΑͲӵTï7ՕӮϰ˶ЫT¾ʣN.f%E;NՕgfsB 2cW gfsC Sµª¹¹ԮƦjˬɐΕΑͲµª¹¹N.f GAP µ ª ¹  ¹ R Г 5 ɺ 1 Օ C- ʿ ϊ R 3xFLAG  z j ɰ Ģ ? G ˗ Օ GAP-GfsB-3xFLAG ˗ 2 c W
GAP-GfsC-3xFLAG ˗jˬϚ?G%ɝ-FLAG ɝójͻ/Gpr·µRceՕGfsB 2cW GfsC SΑͲjέҍAf;O4N5G%ͲƞՕGAP-GfsB-3xFLAG ˗2cW GAP-GfsC-3xFLAG ˗ceϦѱ?G GfsB
2cW GfsC jͻ/MӮϰ̭ȾS˧įj҉^M/f%
Functional analysis of galactofuranose transferase in Aspergillus nidulans
Yukako Katafuchi1ՕSaki Shinozuka 2ՕMinoru Izumi2ՕKeisuke Ekino1ՕKaoru Takegawa3ՕMasatoshi Goto3ՕYoshiyuki
Nomura1ՕTakuji Oka1 Ւ1Univ. of SojoՕ2Univ. of OkayamaՕ3Univ. of KyusyuՓ

P-46
Չё Aspergillus oryzae S·pΑ͢ԅӐӟêǇOΜųȾjίAӟêǇSΑͲ̎ҺǩύŞřą 1Օ͂ӁԒȍ 1ՕèѠѐº 2ՕÓżŌË 3
Ւ1 ηͼΞІԳΧ

Օ2 ǸɗƺӀ¸ǟĬotՕ3 ˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓ)ΚΕ*ՉӏeNTοՉёSә/RcJMՕĳʼ3d̈́ȑ4¼4ebA/ļȽƣOȬ&R̈́ȑ4¼4fļЋ
ƣ4.f%ё˗RcfΑ͢Rԅ¿AfӟêǇΑͲSә/jɇǓ?ՕʛRѾʣ=gM/fΑ͢˦ͧ·pSΑ͢ԅӐӟêǇN.f alternative oxidase ӟêǇՒSrAOXՓO uncoupling protein ӟêǇՒSrUCPaՕSrUCPbՓ
SΜų˧ϱjѦJG%ESϹˌՕ2 οS AOXՒAoAOX2ՕAoAOX7ՓO 3 οS UCPՒAoUCPa2ՕAoUCPa3Օ
AoUCPb5Փjѷį?ՕՉ̈́ȑͨȾS·Qfё˗R29fEgdӟêǇSΑͲRK/M˧҂?G%)ʘ̥*ļȽƣżƎͻՉё AOK209 ˗OļЋƣ AOK139 ˗2cW RIB40 jͻ/MϟՉjöɐ?Օ24 ʪԄO48 ʪԄΚRǓȾ RT-PCR jѦJG%AOK139 ˗SԿ̈́ĮʹRcf DNA ±·¥· Crawler Ʒ·˗SÂ3
d 25R29f͹Х4рǂNϟՉSȋƢ̈́ȑ4ceԿ/˗ AOK139-LT4ՕLT33ՕLT40 jӞɞ?G%24 ʪԄΚSՉ3dғѱ?G total RNA jͻ/M qRT-PCR jѦ/ՕŰӟêǇSҸĩӵ̎ҺjѦJG%)Ϲˌ*ǓȾ RT-PCR NT AoUCPa3 2cW AoUCPb5 4 24 ʪԄΚNΑͲ4ҍ`dgՕ·ȠȑT AOK209
աՠRIB40աաAOK139 N.JG%AOK139 SԿ̈́ƣ Crawler Ʒ·˗ LT4 NT AoAOX7 O AoUCPb5ՕLT33
˗NT AoUCPa2 SҸĩ¼ʢ4EgFgҍ`dgG%=dR LT44 ˗NT 5 οSӟêǇģMSҸĩ̎ͯ4ѻ˗
ceԿ7QJM/G%â¼Օ;gdΑ͢ΜųӟêǇTՉӏeNS̈́ȑ¼ʢRǜ¿?M/f;O4ɷǓ=gG%
Expression analysis of AOX and UCP genes homologous to plant thermogenesis genes in Aspergillus oryzae.
Hironobu Ogasawara1, Takayuki Watanabe1, Kikukatsu Ito2, Katsuya Gomi3
(1Akita Res. Inst. Food & Brewing, 2Cryobiofrontier Res. Center Agri. Iwate Univ., 3Div. Biosci. Biotech. Future
Bioind., Grad. Sch. Agric. Sci., Tohoku Univ.) 58 —P-47
ՊёR29f Ustiloxin B ͹űɐӟêǇy±¹ҸĩƔǇ ustR ԿΑͲRcf
Ustiloxin B ͹ͺŲѷƉ 1Օˡ˄мǇ 2ՕԁӴȈЕ 3Օǩ̗щʣ 2Օ΀ͼԚÇ 2ՕԊӧʍɄ 1,4
Ւ1 ˈŏƺ¸NICHeՕ2 ͺІΧ¸͹ͧµՕ3 ͺІΧ¸CBRCՕ4 ˈŏƺԍӀ¸͹ͧͺ˩ŁɐՓ

Ustiloxin B TՕUstilaginoidea virens RcJM͹űɐ=gf;O4΢dgM/fÑ˹áҚͺͧN.f%ʶӄՕAspergillus flavus R2/MaˀŎűͧSͺ͹4έҍ=gՕǇƑёNTƬźúSQ/ ribosomal peptide synthetic
ՒRiPSՓŎűͧO?MՕES͹űɐRԅ¿AfӟêǇy±¹4ųǓ=gG՘Փ%]GՕՊё A. oryzae R2/MaΜųQӟêǇy±¹4ǉƞAf;Oaʣd3RQJM/f՘Փ%ºʘՕA. oryzae SӴ͹˗R2/MՕ
Ustiloxin B Sͺ͹Tέҍ=gM2dBՕy±¹ħҸĩƔǇՒustRՓŻӁԮƦS˸ɽ4͹űɐĸȯRԅ¿
AfOɷǓ=gM/f%ˀΧσNTՕA. oryzae R2/M Ustiloxin B ͹űɐӟêǇy±¹S˶ЫjѾˊA
fG`ՕustR SԿΑͲ˗jӏɐ?ՕUstiloxin B S͹ͺȾj҈þAf;OjΚΕO?G%]BՕՊёͻԿΑͲµª¹¹ՒPglaA142ՕPenoA142ՓRcJM ustR SΑͲjĸȯ?Օy±¹ħӟêǇSΑͲȺϓjѾˊ
?G%ESϹˌՕCD ʶǩƧƠՕV8 ƧƠR2/MՕustR SԿΑͲRë0y±¹ħӟêǇSΑͲ¼ʢ4έ
ҍN5G%=dRՕCD ƧƠNTͺ͹?Q/4ՕV8 ƧƠ2/M Ustiloxin B Sͺ͹4έҍ=gG%â¼SϹˌ3dՕՊёӴ͹˗R29f Ustiloxin B Sԥ͹ͺRT ustR S˶Ы¾ģ4ԅ¿Af;OՕy±¹ħӟêǇSΑͲ̢ͪH9NQ7ՕƧƠ˖Ըɐİ4 Ustiloxin B S͹űɐRTӳѵN.f;O4ίƅ=gG%
ՒˀΧσTՕϸ̾ͺ˩ΝǄ҃Ð˩'ԧʗΕot¦²m³ǕͲSG`SԿ˶ЫŎ|¨o·əѧԃΑ(SºӧO?MǕʙ=gG%Փ՘ՓUmemura et al., Fung. Genet. Biol., 68 (2014) 23-30.
Production of ustiloxin B by overexpression of the ustR gene in Aspergillus oryzae
Akira Yoshimi1, Myco Umemura2, Nozomi Nagano3, Hideaki Koike2, Masayuki Machida2, Keietsu Abe1,4(1NICHe, Tohoku Univ., 2BRI, AIST, 3CBRC, AIST, 4Grad. Sch. Agric. Sci., Tohoku Univ.)

P-48 (O-5)ΓсаˁёRcf²z·͹İѾRȷԭQӟêǇSųǓR_9GƨΙʏĒÂ̝ ǅÛ 1ՕǗǼ Ǎǥ 2Օˀͼ ¿º 1 Ւ1 Ùƺ¸ӀՕ2 ˥ˋІΧՓ ɣǇёԂRİԲ=gfΓсаˁёTՕҲԞİѾȾԿİǇ²z·jŘͫN͹İѾՒ͜˶ŎՓūЫQƠͳ¼
ƆºS͹ͧN.f՗ԁȌՕES²z·͹İѾRԅifӮϰЖSΧσTΗkRѦigM5G՗ӄȌNTՕŰοt§yѾˊ4ΗkRѦigՕΓсаˁёRԅAf͹ɋ¸ӑŎQPŰʘԦNкż̹/΢ѷ4Ȯdgǃ`M/f՗?3?ÜʜRиJMaՕQDΓсаˁё4²z·j͹İѾN5fS3¸EgjūЫR?M/fÄ
ѵѵϰTǕԕôQS3ՕͨRӟêǇ´¡³NT¼҄ТȶQ͚4¾ʣQ]]N.f՗E;NˀΧσNTՕΓсаˁё±{jͻ/GԬӟêǋՒ²z·͹İѾRȷԭQӟêǇSųǓՓjӍ@MՕ¼҄SҗRӆf;OjΚ˰O?M/f՗ˀΑѫNTՕESǕͲSG`RѦJGο&S˧҂ϹˌRK/MƬźAf՗ ˀΧσNT˧҂ǕԽO?MՕ²z·͹İѾЫOΜԅjίAсϰՒƨҮՓЯсЫjɫ˰O?Gυ͞Ʒ·óy²¹·zjѦJG՗|¨Ѿґ=gՕ×өūЫQªu²t· PC9¸PC15 ԄS F1 ǇǌR2/MՕǍǓΕRЯсЫjĄɪAfƨҮ¸ƧԸ˅åj̙Ǔ?GȫՕPC9 ˗Rǣ?M UV Ʒ·jǨĢ?G՗ϹˌՕϬ 150
˗R 1 ˗SŀűNƨҮЯс¾ģj5GAυ͞Ʒ·ó4ĨͲc7İԝN5G՗˹RՕPC9¸PC15 ԄR29fͨ
ǓS|¨өĲȂ·jՕPCR RcJMϝĀ3KňͯΕRқĵN5fǕԽϪjέχ?G՗F1 İˊR2/MՕƷ·ѫͲƣ4ŘºӟêǇSƷ·RұƔAfOίƅ=gGυ͞Ʒ·ó B84PC15 ԄS F1 ǇǌԛƕjՕ¼҄ PCR
RcfӟêѾˊRü?G՗ϹˌՕͨǓS|¨ԮƦ4ՕƷ·ѫͲƣOȠ7ӐӾ?Mİө=gf;Ojѷ/H?GՒPC9PC15 NTՕE0NTQ3JGՓ՗â¼jҵ]1MͲƞTՕ|¨¸²¹{·jӍ@GƷ·ϕɕSͨǓՕE?MɷǓƷ·ӟêǇSΜѰǕԽRcJMՕŞƔƷ·ӟêǇjͨǓAf;Oj҉^M/f՗
Forward Genetics in the white-rot fungus Pleurotus ostreatus: Towards understanding molecular mechanisms
underlying wood decay
Takehito Nakazawa1, Yasumasa Miyazaki2, Yoichi Honda1 (1Kyoto Univ., 2FFPRI)

 59 —P-49
ɣǇё Phanerochaete chrysosporium ͽˆ PQQ ýǉȾӯŎӡěӮϰӟêǇSyµ¹·z2cWΑͲɓҝĞȋ 1Օˡ͓σ 2ՕΥͼŕË 1ՕŲͼҏ 2ՕÓőǽƟʜǇ 1ՕՃǺ˽̱ 1 Ւ1 ˈƺԍ¸Ӏ͹θՕ2 ӀȀƺ¸ӀՓӄȌՕɣǇё Coprinopsis cinerea 3d PQQ ýǉȾϧҮЯ̒ϰӮϰՒCcSDHՓ4Αѷ=gG%ˀӮϰTՕ¨©o·ՕPQQ jѰӮϰO?Gѿǆ©o·Օ2cWϧҮϹűª­¹³3dˬɐ=gM/f%;Sѿǆ©o·jͻ/G|¨¹¡¹SΜųȾ˧ϱSϹˌՕƹ7SΟ˘͹ͧ4ˀ PQQ Ӯϰjʸ?M/f;O
4ίƅ=gG4Օ˶ЫѾˊ=gGaST C. cinerea ͽˆS^N.eՕßSӮϰRԅAf΢ѷTÈ?/%E;NՕˀΧσNTՕPhanerochaete chrysosporium 3d PQQ Ӯϰ˭ӟêǇSyµ¹·zՕ2cWΑͲѾˊjѦJG%
P. chrysosporium jՕz³}¹2cW ³µ¹j͙ϰ͈O?GƧƠNƧԸ?ՕȮdgGёó3dºˀӾcDNA jűɐ?G%;gjӺƣR?M RACE ̥jͻ/G PCR jѦ/ՕΚΕӟêǇS 5’ʿϊ2cW 3’ʿϊSөĲj̙Ǔ?ՕESȫՕģԁөĲj̙Ǔ?G%;SӟêǇSɷǓm§ӯөĲjՕCcSDH S PQQ ©o·Sm§ӯөĲO̎Һ?GO;hՕPQQ OSϹűRԅ¿AfOÏɇ=gfm§ӯ̄ƨ 5 K4AZMĄǉ=gM/G%]GՕz³}¹ƧƠ2cW ³µ¹ƧƠNųνȑSΑͲ4έҍ=gG%ˀ·yҮS˶ЫѾˊjѦ0G`RՕͲƞՕ©¹³ҪŎȾӮ̋jͻ/G·οǛÄΑͲjѦJM/f%

Cloning and expression of a 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.)

P-50
ɣǇё Phanerochaete chrysosporium Sµz³u·̼Ņňˌ

³±¹Օ

§

³±¹͹ͺR29fw

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)ʘ̥OϹˌ*  j S ³µ¹j͙ϰ͈O?ՕŰοS § ³µ¹šW¢y·w
µz³u·Օw±·Օz³}¦··Օ¢y·j  ̼Ņ?G  ƧƠNɯO0ƧԸ?G% ʪԄ<OR·²·zjѦ/ՕȮdgGёóƸ̶jͻ/MёóƸ·yҮ͕ȑO µq¹³
өϧóSŅ̒İѾ̭ȾjͅǓ?G%wµz³u·j̼Ņ?GƧƠNƧԸ?GƭűNTՕw±·j̼Ņ?
GƭűOų˭RՕ ³µ¹S^j͙ϰ͈OAfƭűR̎ZёóƸ·y͕ȑ2cW wµŅ̒İѾ̭Ⱦ4ԱјRԿ7Qf;O4ʣd3RQJG%]GՕ±ySİѾ̭Ⱦ4w±·j̼Ņ?GƭűO̎Һ?MԿ7Qf;O4ʣd3RQJG%

Effects of xyloglucan on cellulose and hemicellulase production by Phanerochaete chrysosporium
Satoki Kawamura, Akihiko Nakamura, Takuya Ishida, Kiyohiko Igarashi, Masahiro Samejima,(Univ. of Tokyo) 60 —P-51
Aspergillus oryzae ͽˆʗѸQm

³w±·r±¹SͨȴL9ƺƮƨȎՕ͂ӢѯËՕƯӴЗÛՕǩԅŕË ՒǵȢƺ¸ӀՓ)ΚΕ*q³±ӯr±¹.f/Tm ³w±·r±¹T˦ͧϳЩƲ § ³µ¹RǉƞAfq³±ӯ.f/Tm ³ƨOϧSr³ϹűjŅ̒İѾAfӮϰNՕňͯΕQot¦İѾbʸͻQ͹ʹ̭ȾͧҮN.fq³±ӯSɢįRǜ¿?M/f%q³±ӯr±¹TűɐƨҮSq³±ӯ©³(MFA)Օp-y¦³ӯ©³(MpCA)Օuqӯ©³(MCA)Օ2cW·ӯ©³(MSA)RǣAfͨ·ȾOm§ӯөĲSΜŊȾRƨL5o A-D S 4 KRİԲ=gM/f%ÜƓՕAspergillus oryzaeͽˆNo D RΜųQq³±ӯr±¹˭ӟêǇS˶ЫѾˊRK/MΑѫAf%)ʘ̥*A.oryzae SӟêǇɆƬ3do D q³±ӯr±¹RͨȴL9=gGaSOΜųȾS.f
ӟêǇ(Ao090701000884)jyµ¹·Ŏ?ՕPichia pastoris GS115 jͻ/MΑͲ=CG%²}··ӮϰTŰοyµ¦z±n¹RceϦѱ?ՕϦѱӮϰjͻ/MͨȴL9jѦJG%)Ϲˌ*İǇӵT SDS-PAGE NϬ 27kDa NҁϖċO[\ºй?G%ʶӜ pH šẄ́ȑTEgFgՕpH8 2c
W 30NՕpH8-10 SԮƦ2cW 40]NǍǓN.JG%-³r³RǣAf̭ȾNTՕӭӯr
³Rǣ?Mʶa̭Ⱦ4Կ7ՕΣӾSЬФӯr³Rǣ?MṰȾjί?GaSSՕԁӾSЬФӯr³NṰȾjί=Q3JG%q³±ӯr±¹ƨҮRǣAf̭ȾTģ7ί=BՕ·¹ƨҮS̜
ԳǇӯ©³Օ±¡·r±¹ƨҮS 4-µwǍɁԺӯ©³Rǣ?Maų˭N.JG%ºʘՕm ³Ŏ?Gwµ¹2cWz³}¹3dӬӯjӓԝ?Օ]GǩՈ¦3daӬӯjӓԝAfOO
aRՕw±¹OSΜÉňˌaί=gG%cJMˀӮϰTo D Sq³±ӯr±¹Om§ӯөĲTԲí?M/faSSՕo D 3dSʗѸQm ³w±·r±¹OͨȴL9=gG%
Characterization of a novel acetyl xylan esterase from Aspergillus oryzae
Motohiro Otsuka , Yuya Watanabe , Yoshihito Siono , Takuya Koseki(Fac. Agric. , Yamagata Univ.)P-52¦{ՒTricholoma matsutakeՓͽˆ112³±¹ӟêǇS cDNA yµ¹·z1ƺ̡Ȏǔ Օδͼ̩Æ Օ˨ͼͷρ ՕǢ½Ԓƽ ՕΓơɏω 1
Ւ1 ӄΈƺԍ¸ӀȺ͹Ŏ, 2 ƺԇȐƺԍ¸͹žȺ͹ŎՓ¦{(Tricholoma matsutake)ϑS˴ʽRĥ͹?M͹ХAfoS5S;Tё˙ёOŽUgՕ͹ХSG`SϧҮϑjՕё˙jÝ?MȮM/fO=gM/f՗ESG`Օё˙ȢɐёSÛȀƧƠ¼NS͹ХTԥȉRӒ/
H9NQ7Օ··b ³µ¹O/JGƻ͞SƹϧjİѾAfЫŃ4ï7ՕßSа͹ȾS5S;Oų˭S˛Ƨ̥NTÛȀ˛ƧRɐń?M/Q/՗;g]NՕȡΧσǖR2/MTՕ¦{T ³µ¹jİѾA
fӮϰϪO?M˪`MȠ/-z³}¹̭ȾjίA;Ojʣd3R?G4Օ-z³}¹SƨҮO
Qf µt²~ϧjüϼAfr·ƣa?7Trwƣ ³±¹S̭ȾT˪`MȞ/OƬź=gM/f՗ё˙ȢɐёՕͨR¦{S͹ͺAfёóƸ ³±¹RԅAfƬźúT;g]NRQ/;O3dՕɑ&TՕ
Avicel jƨҮO?M¦{ͽˆS ³±¹SŘԝ¸Ϧѱj҉^G՗ESϹˌՕİǇӵϬ 80,000 SӧİϦѱӮϰjȮf;O4N5G՗=dRՕN ʿϊm§ӯөĲѾˊɆƬjƨR BLAST ѾˊRcfΜųȾ˧ϱj
ѦJGO;hՕGH l§²¹3 RǳAf cellulose-binding beta-glucosidase OΜųȾjί?G՗¦{ʇƷ̶óƧƠN 30 ʜԄԤГƧԸ?GˀΧσǖĄǉS¦{ Z-1 ˗Sёϩó3d total RNA jɢį?GȫՕӊҸĩŤȺRce cDNA jűɐ?G՗;S cDNA OөĲɆƬjƨR҅ҁ?G±o¦¹jͻ/M PCR RceՕˀ³±¹ӟêǇjyµ¹·z?G՗ͲƞՕˀӮϰSƺӵŦȮ2cWӮϰŎǋΕҖȾҮSѾʣjΚɫ?ՕӮ̋a?7TƺбёħNS·οΑͲj҉^M/f՗

cDNA cloning of cellulase gene from Tricholoma matsutake.
Hiroki Onuma, Yasuhisa Fukuta, Mizuho Kusuda, Takao Terashita, Norifumi Shirasaka(1Grad-Sch. Agri., Kinki Univ., 2Grad-Sch. Life Env. Sci. Osaka Prefec Univ.) 61 —P-53ͨȴΕQƨҮͨ·ȾjɪKՊёͽˆʗѸz³}¹BglHSӮϰǋΕҖȾҮ͂ӧ ʩՕӷʽ єՕȀѠ÷ӤǇՕ̐ǙɐԒՕÓżŌË (ˈŏƺԍӀ¸͹ͧͺ˩Łɐ)ɑ&TՕՊё(Aspergillus oryzae)|¨ɆƬjěRʾѾˊSʗѸ-z³}¹S˶ЫѾʣj;g]NѦJM5M2eՕÜƓʗGRͨȴΕQƨҮͨ·ȾjɪK-z³}¹jѷį?GSNƬźAf%ɵϱ?GɷǓ-z³}¹ӟêǇjՊё RIB40 ˗S|¨ DNA jӺƣO?G PCR ŤȺNŦȮ?ՕՊёԿΑͲͻ¡y¹pNGA142 RϷ^Ӄ^ՕA. oryzae AOK11 ˗RǨĢ?MɷǓʗѸ-z³}¹ӟê
ǇSԿΑͲ˗jöѱ?G%;S0IՕ̶óƧԸN pNPG jƨҮO?Gԕ̭Ⱦ4˧į=gG BglH RK/MՕΫǍƯˊՕԐot·×ɺyµ¦z±n¹jͻ/MˀӮϰjϦѱ?G%BglH SиӜ̈́ȑՕpH TEgFg 50ՕpH4.5 N.JG%]GՕˀӮϰT 60]NǍǓN.eՕՊёͽˆSӮϰÂʶä́ȑǍǓȾ4Կ3JG%˹RՕƨҮͨ·Ⱦj˧҂?GO;hˀӮϰTűɐƨҮS pNPGՕƻ͞t²~ϧS|·tt¹RԥȉRԿ/ͨ
·Ⱦjί?ՕßSƨҮT[OkPİѾ?Q3JG%BglH TՕʛRƬź?Gų@ՊёͽˆS BglA Om§ӯ´¡³N 62%OՊё|¨RǉƞAf GH3 l§²¹ӮϰSÂNTʶaԿ/ΜųȾjʸ?M/G4ՕBglA
4ƺҞo±¤·Sc0QөϧóİѾ̭ȾjʸAfӮϰN.fSRǣ?MՕBglH T;0?G̭Ⱦjί=BՕÁМSƨҮͨ·ȾRTƺ5Qә/4ѷdgG%BglH SßSҖȾҮjűiCMƬźAf%ՒˀΧσT'ȰкĂӑµz±¨ՒA-STEPՓɵϱo(SºҥO?M JST SǄ҃jŧ9MǕʙ=gG%Փ
Characterization of a novel  -glucosidase (BglH) from Aspergillus oryzae with characteristic substratespecificity
Akira Watanabe, Moe Suzuki, Kanako Kudo, Seiryu Ujiie, Katsuya Gomi
(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ.)

P-54 (O-6)ϩͪё4ϳЩƸRİ̤Af β-¦··İѾRԅ¿AfʗѸ·yҮSѾˊӶǇęȋ 1ՕΥŞϯȤӤ 1ՕʻʷՋѪ 1ՕǵˀψË 1Օļˋ˽Ȝ 1Օƺƭ˽ʧ 1Օǩˋƃƽ 2Օȹ̒ěØ 1ՕŅѠԚƵ 1 Ւ1 Ŵƥƺ¸ӀՕ2 Ŵƺԍ¸͹žӀՓ[ΚΕ] β-¦··T˭&Q˦ͧRŶ]gfԞİѾȾƹϧNՕʾĶͻot¦SºKN.fG`Օotr
¹³SŞʔQPO?M̨Κjԛ`M/f%ɑ&TՕβ-¦··S^jƆºS͙ϰ͈O?MϩͪёAspergillus nidulans j͹Х=CGԕRՕendo-1,4-β-¦·¹OĥRϳЩƸRƹӵR͹ͺ=gf˶Ыʾ΢·yҮՒHPՓjųǓ?G%HP T!CVd\Q)?4M7=1I9f6KJ&Y`PdG N>/A2<;%ˀΧσNTՕϩͪёRcf β-¦··İѾR29f HP Sȧŀjʣd3RAf;OjΚΕO?G%[Ϲˌ2cWЛǡ] hp +" (ΔHP ) M'7fβ-_dZdM C#?7;>%6:;?5
Lf,?*7=%36K;.RbSeTfUbceTA@M C#?7;f,? B
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HP M/=(7;?5LfHP TՕ|³Ŏ?G β-¦··SÄӾjŅ̒İѾCBR β-¦··̶͋SϤȑjƺ57ï½=CG%=dRՕHP O endo-1,4-β-¦·¹j̻űAfOՕβ-¦·¹Rcf β-¦··SİѾ4Ăӑ=gG%;gdS;O3dՕHP T β-¦··İǇԄS̒ϰϹűjıʕ?ՕАЂˬӏjЋ`fė5jɪKry··˭S˶Ыjʸ?M/f;O4Л1dgG% ˀΧσSºӧT͹Χ ·¹'o¡¹¯·ŁįƨήΕΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%
Novel protein involved in β-mannan degradation from filamentous fungus Aspergillus nidulans
Yuhei Kaneko՘, Saaya Ishihara՘, Mai Mochizuki՘ Tatsuya Yamamoto՘, Masahiro Maebayashi՘, Masaharu Ohba՘,Tetsuo Kobayashiՙ, Motoyuki Shimizu՘, Masashi Kato՘ (՘Meijo Univ., ՙNagoya Univ.) 62 —P-55
Պё Aspergillus oryzae SɪKİ̤ƣ££²¹ A2 SӮϰǋΕȾҮSѾˊԿ˓ÕͽЕ 1, ǗǿɦË 2, ƺƮ̺ 2, ͼÇćę 2, ŏˀŌV; 1, ʸǷǋ 1
Ւ1 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹Ȁ, 2 ˈƺԍ¸Ӏ͹θ¸Ⱥ͹ŎՓ)Чʭ*££²¹ A2(PLA2)Tz² µ²·ЬҮS sn-2 îr³ϹűjŅ̒İѾAfӮϰN.eՕŊ
ͧR2/MTΗkRΧσ4ѦigM/f4ՕȲ͹ͧRK/MTՕӮ̋4 PLA2 ӟêǇjɪGQ/G`΢ѷ4È
?7ՕESӮϰǋΕȾҮb͹ʹ˶ЫT[OkPi3JM/Q/%;g]NRɑ&T A. oryzae |¨ÂR 2 K
S sPLA2 t³µz sPlaA O sPlaB jѷį?ՕEgFgS·QfǯƞȾQPjʣd3R?M/f%ˀΑѫN
TՕsPlaA O sPlaB SӮϰǋΕȾҮSѾˊjѦ/ՕsPlaB 4ÏɇƸRa PLA1 ̭ȾjɪK;Ojʣd3R?G%)ϹˌOЛǡ*ƺбёN͹ͺ?GϷɺ1 sPlaA 2cW sPlaB RK/MՕ1-³§o³-2-[14C]t´to³-£l³}²·(PC)jƨҮRͻ/Gm ojѦJGO;hՕsPlaA RK/MT PLA2 ̭ȾRͽˆAf[14C]t´o·ӯS͹ɐ4ҍ`dgG4ՕsPlaB NTÏɇƸRa PLA1 ̭ȾRͽˆAf 2-[14C]t´to³² PC
OЛ1dgf¥4˧į=gG%¦¢yµ©²¹RcfͅǓR2/Ma¼ӇSϹˌOºй?G¹y4˧į=gG%;gdSϹˌ3dՕsPlaA TөĲ3dÏͅ=gGӍe PLA2 ̭ȾjɪKSRǣ?ՕsPlaB
T PLA2 St³µzN.fRaԅidB PLA1 ̭ȾjίA;O4i3JG%=dRՕsPLA2 R2/MĄǉ=gG̭ȾÂȶ̄ƨN.f·jm±·RГɺ?GƷ· sPlaB ·yҮjöѱ?Օ[3H]t´o·ӯ˰қ?Gƺбёг΁İjƨҮO?Gm ojѦJGO;hՕ̭Ⱦ4ѷdgQ7QJG%;S;O3dՕsPlaBSɪK PLA1 ̭Ⱦ4ßS sPLA2 Oų˭Sѿǆ˶ˬRcfaSN.f;O4ίƅ=gG%
Analysis of two secretory phospholipases A2 in Aspergillus oryzae
Ayumi Takayanagi1, Takuya Miyakawa2, Jun Ohtsuka2, Masaru Tanokura2, Katsuhiko Kitamoto1, Manabu Arioka(1Dept. of Biotechnol., The Univ. of Tokyo; 2 Dept. of Appl. Biol. Chem., Univ. of Tokyo)

P-56
ՌՊё Aspergillus oryzae pepO ӟêǇ˸ɽ˗SёóƸr·ƣµm¹RK/M¼ӴϻǇ, ļͼ̱, ǵȢ̫ȋ, όħӗԙՒӀȀƺԍ¸Ⱥ͹ŎՓ)ΚΕ*|¨ѾˊSϹˌՕՌՊё A. oryzae RIB40 RTӯȾ˅å½Nöͻ?¢·Rԉǘ=gfr·ƣµm¹N.fm³nyµm¹ՒAPaseՓj}¹AfOɷǓ=gfӟêǇ4 11 ĈǉƞAf;O4ʣd3OQJG%;S 11 S APase T̶ЩǯƞՕгǯƞՕёóƸİ̤ƣS 3 οRİԲ=gf;
O4ɷͅ=gM2eՕpepO ӟêǇT 5 K.fёóƸİ̤ƣS0ISVOKN.f%âļSƬźceՕAPaseӟêǇAZMN mRNA Sǉƞ4έҍ=gՕҸĩ=gM/f;O4ίƅ=gG%ESºʘNёóƸR2/M
·yҮO?M˧į=gGST PepO S^N.JG%â¼SϹˌjŧ9ՕˀΧσNTpepO jöѱ?ՕES
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·Rcfԉǘjŧ9BՕ]GՕ̄ǉ̭ȾSÄQaST antipain RceȠ7ԉǘjŧ9f;O4ʣd3O
QJG%antipain Rԉǘ=gӯȾNöͻAfr·ƣµm¹N.f AorsinA SƨҮ Z-Arg-Arg-MCA R
ǣ?MՕAMC jӓԝAf̭Ⱦ4ҍ`dgG%â¼S;O3dpepO ˗TӯȾNöͻAf AorsinA j͹ͺ?
M/f;O4ʣd3RQJG%pepOaorsinA jöѱ?G%;S˗O RIB40 SӯȾNöͻAfr·ƣµm¹RK/M˧҂?M/f%
 Q2$ˀΧσSºӧT͹Χ ·¹ƨήɷӑÐ˩Sº͸O?MѦigGaSN.f
Analysis of extracellular endoproteases in Aspergillus oryzae pepO gene deletion strain
Ayako UENO , Hiroshi MAEDA , Youhei YAMAGATA , Michio TAKEUCHI(Division of Applied Biological Chemistry,Tokyo Univ. of Agriculture and Technology) 63 —P-57
Emericella variecolor R29f

³¢·űɐӮϰSɵϱ»˵ԒωՕˉͼûƺՕ̸ǿǊЗՕԊӧӥʺ Ւˈƺԍ¸џՓ
5 KS͙ϰ3dQfo´·ŘîjESˬɐŘîOAf³¢oTƻ͞Rƺ5QŀűjŚ`fŎűͧЖN.f4Օ;SÂR.JM 5 KSo´·ŘîRͽˆAf ³¢·ԲTƬźúSǪQ/̎ҺΕμQŎűͧЖO?M΢dgf%Ņ1MՕ ³¢·ԲR2/MTES͹űɐϸҴRԅ?MaʾHΧσú
4ǪQ/%E;NˀΧσNTՕ ³¢·͹űɐԅӐӮϰӟêǇSųǓOES˶ЫѾˊRŦeϷ_;OO?G%ʡѡՕԿϑ˦ͧՕ̳ЅŊͧQPȊȎ/͹ͧο3dSŘԝƬź4.f ³¢·N.f4ՕϩͪёaE
SÄѵQ͹ͺМSVOKO?M΢dgM/f%ɑ&TՕƹ˭QԾ˚QdWR͹̭ͧȾjʸAf ³¢·ԲSŘԝ4Ƭź=gM/fϩͪё Emericella variecolor RΠΚ?Օ|¨¦o·zSɗ̥jͻ/MˀёS|¨ɆƬ3d ³¢·űɐӮϰӟêǇj˧ϱ?G%Ņ1MՕϩͪёSÑ˹áҚͧS͹űɐRԅifӮϰӟêǇT|¨¼NǯƞŎAfĕŵR.f;O3d ³¢·űɐӮϰӟêǇSŻӁԮƦj˧ϱ?Օ³¢·SĆԷRԅifOÏɇ=gfӮϰӟêǇjѷį?G%;gdӟêǇS˶ЫѾˊTՕ·οϩͪё Aspergillus oryzae RMΑͲϪjˬϚ?ՕESáҚͧjѾˊAf;
ORcJMѦJG%ESϹˌՕC25H40 SİǇȚjɪK͸ͪ³¢ojͺͧO?M¿1f ³¢·űɐӮϰӟêǇSŦȮRɐń?G%]GՕES͸ŎͺͧTȡҊӟêǇSӄđRǉƞAfyµ¨ P450 R
cJMʛ΢ ³¢·N.f stellatic acid YOƷɺ=gf;OaĴʣ?Օstellatic acid ͹űɐSİǇƨΙjʣd3RAfRиJG%
The search for sesterterpene synthases from Emericella variecolor
Takaaki Mitsuhashi, Yudai Matsuda, Takayoshi Awakawa, Ikuro Abe(Graduate School of Pharmaceutical, Univ. of Tokyo)

P-58
o{(Lentinula edodes)R29f GABA ͹ɐRԅ¿AfӮϰRK/MǸˀſǇՕδͼ̩ÆՕΓơɏωՒӄΈƺ¸Ӏ¸Ⱥ͹ŎՓ-m§ӭӯ (GABA) Tз͞΂RȎ7İȇAfԥ·yҮˬɐm§ӯSºοN.e, ѥƝ¼ʢɛĸöͻ, ĶǮöͻ, ϧǮΎSÏԈQPRňˌ4.fO/igM/f;O3d, ӄȌ, ˶ЫȾԳƀϰ˃O?M̨Κjԛ`M/f%ºоΕR GABA T²w¹³ 5’-²·ӯýǉӮϰN.fz³§·ӯu³¤w±¹
 (GAD) Rcf L-z³§·ӯSЯ͙ӯŤȺRcJM͹ɐ=gf;O4ʣd3RQJM2e, ;g]NRŊͧ, ˦ͧ, ϳё, ёԲͽˆS GAD 4Ϧѱ=g, ESȾҮ4Ƭź=gM/f%ºʘ, Գͻ5S;R2/Ma
GABA 4ƹ7Ŷ]gM/fO/0Ƭź4.fRaԅidBŶӵb͹ɐϸҴRK/MҋϳR˧҂=gGúTǪ
Q7, Գͻ5S;jŶ_ɣǇёͽˆ GABA њςRԅ¿AfӮϰRK/MSƬźTǪQ/%E;N, Գͻ5S
;ÂS GABA Ŷӵjʣd3RAfOĥR, GABA ͹űɐRԅ¿AfӮϰjϦѱ?, ESȾҮjʣd3RAf;Oj҉^G%Ȇңo{ǇǕój 50mM Ӭӯl¹(pH4)OĥRΩΨȫ, ӛȶİԝceȮdgG¼̽jΫǍƯˊ,
Ԑot·×ɺyµ¦z±n¹, ԑot·×ɺyµ¦z±n¹jͻ/MϦѱ?, ťͯ 7.14%, Ϧѱĉͯ9.28 ĉN, Ԡ̪̑ŊΕRŘºSӮϰjȮG%ϦѱӮϰSİǇӵT SDS-PAGE ceϬ 49kDa, HPLC-GPC ceϬ
131kDa N.JG;O3d, ˀӮϰTÑӵóN.f;O4ίƅ=gG%ʶƺ̭ȾT 37, 37]ṊȾTǍǓ
N.JG%ϦѱӮϰSħӧm§ӯөĲjѾˊ?, ΜųȾj˥ˋІűΧσɕceɸü=gM/f ForestGEN
S Lentinula edodes ¹¡¹ħN˧ϱ?GO;h, phosphatidyl serin decarboxylase (psd)O 100%SΜųȾjί?G%]G, psd ӟêǇSƯƨөĲjƨR±o¦¹j҅ҁ?ՕcDNA yµ¹·zjѦJG%
Study on the enzyme related with GABA formation in Lentinula edodes
Kazuko Iwamoto, Yasuhisa Fukuta, Norifumi Shirasaka(Div. Appl. Biochem., Agr. Sci, Kin-ki Univ.) 64 —P-59
·Qf̈́ȑNƧԸ?G Aspergillus fumigatus ЩǇS̎Һ±·y²¹¨ѾˊѕŞƺα 1ՕӫÔԺǀ̖ 1ՕӷʽП 2ՕÍÔğȣ 1ՕÓÔӋ 1Օǿˀӑ 1 Ւ1 Œїƺ¸Οё·¹Օ2 ԳІΧՓ ΎŞΟё Aspergillus fumigatus TЦm¢³x³ΏSÄѵQŞƔёN.eՕЩǇTӳѵQɊˑƔǇN.f%
͸ưÂRӕƞAfЩǇTՕǕԽǖR29fƢҮQƧԸNΠ͹?GaSOT·QeՕз͞͸ưÂSƹ˭Q˅å
SaONΠ͹?GaS4̻ƞ?M/f%E;Nɑ&TՕƧԸ˅åSә/RceΠ͹AfЩǇSҖȾҮ4ƷŎ
AfO/0ãҐjχM˧҇?G%ˀΑѫNTƧԸ̈́ȑSȦԪj˧҂?M/f%ʶӜƧԸ̈́ȑN.f 37RŅ1MՕ͹Хӎȑ4ï½Af 252cW 45R2/MՕA. fumigatus j PDA R
˦1M 7days ƧԸȫSЩǇjƓť?G%25ƧԸNƓť?GЩǇՒ25ЩǇՓTßS҉ʔR̎ZM͕/͗ЇсjŹ?ՕUV Rǣ?MęōQНȾjί?G;O3d©±·ӵSƱŅ4ίƅ=gG%=dRՕ25ЩǇTßS҉ʔR̎ZM͢´Rǣ?MɊŧȾ4Ʊƺ?M2eՕЩǇħS´µ¹ӵáǪ?M/fÐ4i
3JG%ƧԸ̈́ȑRcfȦԪj|¨¶oRʹѾAfG`ՕЩǇħS mRNA 3d RNA-sequencing Rcf
±·y²¹¨ѾˊjѦJG%ESϹˌՕ՘Փ37SƧԸR2/MёϩOЩǇON̎ҺAfO 1079 ӟ
êǇ4ЩǇͨ·ΕQΑͲjί?G%ՙՓ©±·űɐϪӟêǇЖSΑͲT 25ЩǇNԱјRԿ/ċjί?G%՚Փ25ЩǇNͨ·ΕRΑͲ?M/fÑ˹áҚy±¹jѷį?G%ͲƞՕ25ЩǇRͨ·ΕQÑ˹áҚ
y±¹ħRŶ]gf PKS OɷǓҸĩĸȯƔǇSӟêǇΩƳ˗jöѱÂN.eՕˀy±¹ħSҸĩĸȯ©u¨SѾʣbʶ϶ͺͧSųǓjΚɫ?M/f%
Comparative transcriptome analysis for conidia harvested from different culture temperatures
Daisuke Hagiwara1, Kanae Sakai, Satoshi Suzuki2, Katsuhiko Kamei1, Tohru Gonoi1, Susumu Kawamoto1
Ւ1MMRC, Chiba Univ., 2NFRIՓ

P-60
ΓՊёR29fɷǓҸĩĸȯƔǇ NosA O RosA SѾˊÑβ̩ƨ 1Օͼáʰŭ 2ՕˤŞȔř 3ՕԿ½εʧ 3Օόǿў 2ՕͰГǫȳ 1ՕȫѠ˽Ķ 2Ւ1 ՇġǺƺ¸ӀՕ2 Êƺԍ¸ӀՕ3 »ſӫԲՓĝΧσR2/MՕՈՊӏeR29fΓՊё Aspergillus kawachii S DNA ¦oyµm´oRcfӟêǇΑͲѾˊjѦJG%ESϹˌՕѱՊӖνՒ403d 30˚C YSƧԸ̈́ȑï½ȫՓR2/MԱјRΑͲƷŊAfӟêǇSÂRɷǓҸĩĸȯƔǇj}¹Af nosA O rosA jųǓ?G%NosA O RosA TՕª³ϩͪё Aspergillus
nidulans R2/MTʸȾ͹̅Rԅ¿Af;O4Ƭź=gM/G%?3?ՕΓՊёRTʸȾÀáTѷį=gM/
Q/G`Օ;gdSɷǓҸĩĸȯƔǇ4ΓՊёR2/MPSc0Q͹ʹ˶ЫjaKS3Rкż4aGgMѾ
ˊjѦJG%]BՕnosA O rosA SŘͫӟêǇΩƳ˗Օ2cWÑӳӟêǇΩƳ˗jˬϚ?G%;gdSё˗SѫͲƣjѼǡ?GϹˌՕnosA ΩƳ˗O rosA ΩƳ˗TӴ͹˗Oų˭SѫͲƣjί?G%ºʘՕnosA rosA ÑӳΩƳ˗TՕİ͹ǇȢɐЫ4Ӵ͹˗SϬ 20%Rï½?G%˹RՕŰӟêǇΩƳ˗jǛÄO?MՕTet-On ΑͲҎǨ¨
Rce NosA-GFP 2cW RosA-GFP jΑͲAfΜѰ˗jˬϚ?G%ѣĞԱȲӿRcfѼǡSϹˌՕNosA-GFPO RosA-GFP T˘RǯƞAf;O4ίƅ=gG%â¼SϹˌceՕNosA O RosA TΓՊёR2/M͹ǇȢɐRԅifӟêǇΑͲĸȯRԅ¿AfūЫȾ4ίƅ=gG%

Characterization of putative transcription factors, NosA and RosA, in Aspergillus kawachii
Taiki Futagami1, Satoshi Tashiro2, Yasuhiro Kajiwara3, Hideharu Takashita3, Kaoru Takegawa2, Hisanori Tamaki1,
Masatoshi Goto2 (1Kagoshima Univ., 2Kyushu Univ., 3Sanwa shurui Co. Ltd) 65 —P-61ӸȿȉȾRԅifҸĩƔǇ HapX O CCAAT-box ϹűƔǇ HapB/C/E OSΜÒöͻÂ˄ԘÛՕӶǇęȋՕȹ̒ěØՕŅѠԚƵ ՒŴƥƺǋ¸ӀǋӧՓ[Чʭ¸ΚΕ]HapX TՕɑ&SΧσz³¹4ĳ`M CCAAT-box ϹűƔǇՒHapB/C/E ѲűóՓOΜÒöͻAfƔǇO?
Mѷį?GΟёԲRͨʸSҸĩƔǇN.f%HapX TӸ˸ÈʪRӸjŶ_·yҮSӟêǇΑͲjɛĸAf
QP?MՕӸSȿȉȾЂɪ˶ˬSÂȶΕQȧŀjˌG?M/f%ɑ&TʛRՕHapB/C/E Ѳűóǉƞ½NS
HapX S DNA Ϲű˭ȚRK/MSΧσjҋϳRӑ`M5G%ÜƓT HapX O HapB/C/E ѲűóOSΜÒöͻSİǇ˶ˬjʣd3RAf;OjΚΕO?G%ˀΧσNTՕAspergillus nidulans R29f HapX S HapB/C/E
ѲűóOSɷǓΜÒöͻ©o·RΠΚ?ՕHapX O HapB/C/E ѲűóOSΜÒöͻj in vivoՕin vitro ÁԦ3dҋϳRѾˊ?G%[ʘ̥¸Ϲˌ]HapB/C/E ѲűóOSɷǓΜÒöͻ©o· (HCI ©o·) j˸ƿ=CGƷ· hapX ӟêǇjöѱ?ՕhapX
˸ƿ˗ՒΔhapX ˗ՓjȢҮҸɺAf;ONՕHapX S HCI ©o·˸ƿ˗ՒΔhcid ˗Փjöѱ?G%HCI ©
o·j˸ƿ=CG Δhcid ˗TՕΔhapX ˗Oų˭RӸĸԌ½NS͹Х4ј?7Ʌ7QJG%;S;O3dՕ;S©o·4 HapX S˶ЫRӳѵQė5j?M/f;O4ί=gG%=dRՕHCI ©o·S˶ЫjҋϳR
ғZfG`RՕEgFgS²}···yҮjƺбёRΑͲ=CϦѱ?G%Ϧѱ?G²}···yҮjͻ/MՕ|³ª²n¹m ojѦJGO;hՕHCI ©o·j˸ƿ=CGƷ·HapX TՕӴ͹ƣS HapX R̎Z HapB/C/E ѲűóOSΜÒöͻ4ј?7ï½?M/G%â¼SϹˌceՕHCI©o·4 HapB/C/E ѲűóOSΜÒöͻRȷѵN.f;O4Ƞ7ίƅ=gG%
Interaction of HapX, involved in iron homeostasis, with the fungal CCAAT-binding factor, HapB/C/E complex.
Hayato Nakamura, Yuhei Kaneko, Motoyuki Shimizu, Masashi Kato (Faculty of Agriculture, Univ. of Meijo)

P-62 (O-9)ՊёSҸĩƔǇ FlbC TƙóƧԸͨ·ΕΑͲjίAz³}m§±¹ӟêǇՒglaBՓSΑͲjĸȯAf
Ų˄ЇՕͼÂͷȃՕʗҝǫȜՕÓż ŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓՊёSƙóƧԸͨ·ΕR͹ͺ=gfz³}m§±¹ GlaB TՕёϩɐԁԉǘ˅åՕï̒İ̭Ⱦ˅åՕԿ̈́ƧԸ˅åO/0 3 ˅åRce´¹ƧԸNaҎǨ͹ͺ4ūЫN.f%;S˅åj͇GAƧԸ˅åO?MՕ
50%¦³¹jŶ_ǟƻƧƠՒï̒İ̭ȾՓRһCGoµ·г¼ՒёϩɐԁԉǘՓNՊёjƧԸ?Օ
oµ·гRİ̤ŷΠ=gG GlaB jɝóŤȺNĨͲȾԿ7˧įAf;ORɐń?G%;Sʘ̥jͻ/MҸĩƔ
ǇΩƳ˗±o±²¹434 ˗Sy²¹·zjѦ/ՕӞɞ?G 19 ˗RK/MǩՈXA]jͻ/GƙóƧԸjѦ/Օz³}m§±¹̭ȾO α-m§±¹̭ȾjͅǓ?G%ESϹˌՕα-m§±¹̭ȾRǣAfz³}m§±¹̭Ⱦ4 glaB ΩƳ˗Oųνȑ]Nï½?G˗4 1 ˗ȮdgG%;S˗Tİ͹ǇȢɐRԅif;O4Ƭź=gM/f C2H2 ƣҸĩƔǇ FlbC SӟêǇΩƳ˗N.JG;O3dՕFlbC Oų˭SϸҴN˶ЫAfßSҸĩƔǇΩƳ˗RK/M GlaB ͹ͺjғZG4ՕԱјQ͹ͺï½Tҍ`dgQ3JG%=dRՕGlaB Oų˭RƙóƧԸNͨ·ΕR͹ͺ=gfµm¹Oµ¹jͅǓ?GO;hՕflbC ΩƳ˗NTӯȾµm¹̭ȾSï½4^dgՕFlbC T GlaB SΑͲH9NQ7ӯȾµm¹ӟêǇSΑͲRaԅ¿A
fūЫȾ4ίƅ=gG%
ՒˀΧσT'Ӏˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%Փ

The Aspergillus oryzae transcription factor FlbC involved in the expression of the glaB gene specifically
expressed in solid-state culture
Midori Yoshimura, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi
(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric., Tohoku Univ.) 66 —P-63
Aspergillus oryzae ҸĩƔǇ XlnR/AraR RcfҸĩĸȯ˶ˬSѾˊΥǿԺŗՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ͹žӀ¸͹ͧ˶ˬՓ)ΚΕ*XlnR O AraR T Aspergillus ǳϩͪёSaK Zn(II)2Cys6 ƣSҸĩƔǇN.eՕ/Bga¢·¹áҚϪӟêǇЖj˽RĸȯAf%/7K3SӟêǇT XlnRՕAraR ţʘRceĸȯ=gM/f4ՕES˶ˬ
TʾHʣd3OQJM/Q/%E;NˀΧσNTՕm±¹áҚϪӮϰj}¹Af lxrAՕxdhAՕxkiA
Sµª¹¹ԮƦRǉƞAf XlnRՕAraR SϹűӧîjųǓ?G%]GՕ¢·¹áҚϪSώºSӮϰj}¹Af larA šW XlnR ĸȯ½ӟêǇN.f xynF1 Sµª¹¹ԮƦRǉƞAf XlnRՕAraR ϹűөĲjƨ͉O?ՕXlnRՕAraR EgFgSϹűөĲSзͽȑjѾˊ?G%)Ϲˌ¸Лǡ*ƺбёjǛÄO?M͹ͺ?G XlnRՕAraR S DNA Ϲű©o·jͻ/ՕlxrAՕxdhAՕxkiA
µª¹¹RǉƞAf DNA ϹűӧîjųǓ?GO;h AraR T lxrA NT 1 ϕɕՕxdhA NT 2 ϕɕ xkiA N
T 1 ϕɕS 5’-CGGNNA(A/T)(A/T)-3’O/0}· ·өĲRϹű?, XlnR aųөĲRϹűAf;O4ίƅ=gG%;gjŧ9 xdhA µª¹¹RǉƞAf AraR ϹűөĲjµ¹O? XlnRՕAraR ĥǉƞ½NS
ϹűS˭Ǉjέҍ?GO;hՕXlnR O AraR 4ųʪRϹűAf;OTQ3JG%;gTÁМSϹű4ϋűAf;Ojί?M/f%larA µª¹¹ħS AraR ϹűөĲO xynF1 µª¹¹ħS XlnR ϹűөĲjͻ/
M XlnRՕAraR SϹűөĲSзͽȑjѾˊ?GϹˌՕAraR ͨ·ΕՕXlnR ͨ·ΕՕQdWRÁМĥʸSϹűө
Ĳ4ǉƞAf;O4ʣd3OQJG%]GՕXlnR Rԅ?MTՕөĲRcJMϹűİǇʎ4ƷŎ?G%;gd
TiB3QƯƨөĲSә/RceՕϹűӧîSҸĩĸȯ˶Ы4ƺ57ƷŎAfūЫȾjίƅ?M/f%ˀΧσTՕ͹Χ ·¹So¡¹¯·ŁįƨήΕΧσɷӑÐ˩OӀˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩SºҥO?MѦigGaSN.f%
The mechanism of regulation by XlnR/AraR in Aspergillus oryzae
Kana Ishikawa, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi(Graduate Sci. of Bioagric. Sci., Nagoya Univ.)

P-64 (O-8)
Functional binding characteristics of ManR/ClrB to regulate cellulase and mannanaseproduction in Aspergillus nidulans
Nuo Li, Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi(Grad. Sch. Bioagric. Sci., Nagoya Univ.)
 ManR in Aspergillus oryzae and ClrB in A. nidulans, which are orthologous to each other, were identified
independently as transcriptional activators involved in mannanase and cellulase genes. Cellulase genes are under control
of not only ManR/ClrB but also McmA that contributes to activation of cellulase genes via recruiting ManR/ClrB to
CeRE (Cellulose Responsive Element). In the case of mannanase genes, McmA is generally not required. It has beenshown that ManR binds to the promoter region of mndB that encodes β-mannosidase without assistance of McmA.
To identify the functional binding site for ManR in vivo, DNA fragments of three binding sites (CGGN8CCG) on the
mndB promoter were independently fused to the coding region of A. oryzae α-amylase gene (taaG2) and integrated at
the argB locus of A. nidulans genome. The transformants that exhibited highest amylase activity in response to cellulose
carried the sequence CGGAGCGAAACCCG that located at -547 ~ -560 relative to the translation start site of mndB,
which indicated that this region works as the recognition site of ManR in vivo. Meanwhile, the recognition sequence of
ManR on the promoter of the endoglucanase gene eglB was examined in vitro by supershift assay. The ManR-McmAbinding site of eglB consists of two overlapped CeRE in the opposite direction (CCGN2CCN6GGN2CGG). Mutation of
CCG and CGG led to stronger binding of McmA and loss of McmA assisted ManR binding. This implies that ManR
binding to CeRE is supported by interaction with McmA as well as the CGG triplet. All above discoveries will help tounderstand the binding property of ManR that involved in regulatory function.
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.

 67 —P-65Պё¦³¹ҪŎӟêǇy±¹Sm§±¹ҎǨ͹ͺYSԅ¿ȆǿʠĦՕԁҝǿՖƥγǇՕͼÂͷȃՕʗҝǫȜՕÓżŌË Ւˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՓ)Чʭ*Պё Aspergillus oryzae Tm§±¹jǃ`OAf··İѾӮϰjƹӵR͹ͺAf;O3dՕ̽ӫӱӏRĶͻ=gM/f%ՊёR29fm§±¹SӟêǇΑͲRTҸĩƔǇ AmyR 4ԅ¿?M2eՕAmyR
T¦³¹Օo¦³¹RcJM̭ȾŎ=gfaSOЛ1dgM/f%ESG`m§±¹͹ͺRTҎǨƨҮN.f¦³¹SϳЩħYSŦeӃ^4ӳѵQӖνN.fOЛ1dgf%ՊёR2/M¦³¹
±·¥¹¹MalP TҸĩƔǇ MalR Sĸȯjŧ9M/f%E;N malP ΩƳ˗ՕmalR ΩƳ˗jöѱ?Օ
¦³¹ҪŎӟêǇSm§±¹͹ͺYSԅ¿jѾˊ?G%)Ϲˌ*··j͙ϰ͈Rͻ/G´¹m ojѦJGϹˌՕmalP ΩƳ˗2cW malR ΩƳ˗R2/
M͹ХSɅŎ4Ѽǡ=gG%]GՕÁΩƳ˗OaR¦³¹̶óƧƠR29fm§±¹SҎǨ͹ͺS
ï½4Ѽǡ=gG%ųʪRƧƠÂS¦³¹͕ȑjͅǓAf;ONՕёóħYS¦³¹SŦeӃ^SͅǓjѦJGϹˌՕ;gdSΩƳ˗N¦³¹SŦeӃ^SӒȗ4ҍ`dgG%ͨR malP ΩƳ˗Nm§±¹͹ͺSï½Օ2cWŦeӃ^Ӓȗ4ԱјN.JG%;S;O3dՊёSm§±¹͹ͺRT¦³¹
±·¥¹¹Rcf¦³¹SŦeӃ^4ӳѵN.f;O4ίƅ=gG%

Involvement of maltose-utilizing (MAL) cluster in inducible production of α-amylase, in Aspergillus oryzae
Takanori Ichikawa, Sachiko Hasegawa-Shiro, Mizuki Tanaka, Takahiro Shintani, Katsuya Gomi
(Div. Biosci. and Biotechnol. FutureBioind., Grad. Sch. Agric., Tohoku Univ.)

P-66
ՌՊё Aspergillus oryzae pepO ӟêǇS cis-element SɵϱǵǼŻȋ, ļͼ̱, όħӗԙ, ǵȢ̫ȋ (ӀȀƺԍ¸Ӏ))ΚΕ*RNA-Seq Rcf A. oryzae RIB40 R29fёóƸİ̤ƣm³yµm¹ӟêǇSҸĩ
ѾˊSϹˌ, ǩՈ¦ƙóƧƠR2/M, r·ƣµm¹j}¹Af pepO 4ʶaԿ/Ҹĩӵj
ί?G%ESG` pepO ӟêǇ¼̮RTҸĩĂӑRǜ¿Af cis-element 4ǉƞAfOЛ1dgG%ˀΧσNT, pepO µª¹¹S cis-element SųǓjΚΕO?M, amylase »ӳΩƳ˗jǛÄRͻ/, α-amylase j´¥¹¹O?G´¥¹¹m o̥Rce pepO Sµª¹¹̭ȾjғZf;OO?G%]G, amylase»ӳΩƳ˗jͻ/G´¥¹¹m o̥jέχAf;OaΚΕO?M/f%)ʘ̥¸Ϲˌ*pepO µª¹¹S cis-element jʣd3OAfG`, pepO ¼̮ 2,000 bp 3d 500 bp BK
˸ƿ=CGөĲO α-amylase ӟêǇjӐϹ?G±§jöɐ?, amylase »ӳΩƳ˗RǨĢ?G%ͭȮ?
G 4 οS α-amylase ΑͲ˗RK/M, pepO µª¹¹̭Ⱦj̎ҺAfG`, amylase ̭Ⱦj°pϰ··ŤȺRceͅǓ?G%ESϹˌ, pepO ¼̮ 1,000 bp jӐϹ?G˗S amylase ̭ȾT, 1,500 bp jӐϹ?G˗O̎Һ?MϬ 4 İS 1 R]ŃǪ?G%;S;O3d, pepO ¼̮ 1,500 bp 3d 1,000 bp SԄR pepO
SҸĩj˽RĸȯAf cis-element 4ǉƞAf;O4ίƅ=gG%Ͳƞ, cis-element jϺeӃ_G`R pepO µª¹¹ 1,500 bp 3d 1,000 bp j 100 bp BK˸ɽ=gG˗RK/MѾˊjӑ`M/f%
Identification of cis-elements for pepO in Aspergillus oryzae
Shuhei YAMAZAKI, Hiroshi MAEDA, Michio TAKEUCHI, Youhei YAMAGATA(Division of Applied Biological Chemistry, Tokyo Univ. of Agriculture and Technology) 68 —P-67ϩͪё Trichoderma reesei Sm±x·ӯµm¹SΑͲҎǨ˶ˬSѾʣƯǱȍ˴ՕԟΟȜՕñѠʧђՕȹͼ̫Ý, ǩύŞ̿ ՒԁǷəθƺ¸͹ͧՓϩͪё T. reesei R2/MՕ ³µ¹¸w±·ϪҎǨͧҮRcf ³±¹¸ § ³±¹ΑͲҎǨ˶
ˬ4Ȏ7Χσ=gM/f%;gdSӟêǇSҸĩĸȯR2/MÂȶΕQȧŀjɣ0ҸĩƔǇ Xyr1 4Ƭź=g
M/f%ºʘՕT. reesei 4з͞΂N͹ХAf͸ưÂRT˭&Q˖Ը͈4ǉƞ?ՕEgdRȺϓ?MҎǨ=gf
ʾ΢S·yҮΑͲ˶ˬSǉƞ4Л1dgM/f%;g]NR T. reesei j˭&Q˦ͧϳЩƲˬɐɐİj͙
ϰ͈O?MƧԸjѦJGϹˌՕŘϧNԿ/ҎǨȾjί?Gm±x·ӯµm¹ՒTrAsPՓjųǓ?G%ˀΧσNT TrAsP SΑͲҎǨ˶ˬSѾʣjѦJG% TrAsP SҎǨTՕŘϧSQ3Nav±y¹NaJOaȠ7ҎǨ=gf;O4ί=gG%E;NՕv±
y¹O ³±¹ҎǨƨҮN.fsµ¹j͙ϰ͈O?GO5SҎǨǕԽjѦJG%ESϹˌՕv±y¹N ³±¹ԅӐӟêǇЖ4ҎǨ=gQ/SRǣ?ՕTrAsP TȠ7ҎǨ=gM/G%ºʘՕsµ¹ҎǨNTՕ ³±¹ԅӐӟêǇЖTҎǨ=gM/G4ՕTrAsP TҎǨ=gQ3JG%˹RՕÁƨҮ
ǉƞ½NҎǨǕԽjѦJGϹˌՕ ³±¹2cW TrAsP SΑͲӵŚǪ4έҍ=gG%]GՕ˭&Qφϰ
͈jͻ/Mų˭QǕԽjѦ/ՕTrAsP 4φϰ͈ͨ·ΕՒͨR BSAՓNҎǨ=gf;Ojέҍ?G%?3?Օ
BSA Ov±y¹jŶ_ƧƠNҎǨǕԽjѦJGO;hՕTrAsP SΑͲӵT BSA Řͫceï7QJG%;
gdS;OceՕTrAsP SΑͲTv±y¹NȠ7ҎǨ=gՕʛ΢S ³±¹ΑͲҎǨ˶ˬOT·Qf
ĸȯ½R.f;O4ίƅ=gG%]GՕv±y¹Rcf TrAsP SΑͲҎǨ˶ˬTφϰ͈RcfΑͲҎǨ˶ˬOa·Qf;Oaίƅ=gG%=dRՕ¦oyµm´ojͻ/M TrAsP OŖғΕRΑͲAfӟêǇSɵϱjѦJGϹˌՕTrAsP Oų@ΑͲ¹·jίAµm¹Sǉƞaίƅ=gG%
Transcriptional mechanism of Trichoderma reesei aspartic protease
Koki Shioya, Masahiro Yuki, Haruna Sato, Yosuke Shida, Wataru Ogasawara(Dept. of Bioeng., Nagaoka Univ. of Tech)

P-68
Aspergillus nidulans
Ѿˊ

³±¹¸

§

³±¹SΑͲRԅif±·¥¹¹S

ƛ˾ϾЕՕӶÃÙǇՕʽ˄ΟՕǩˋƃƽ ՒŴƺԍ͹žӀ¸͹ͧ˶ˬՓ
Aspergillus nidulans T ³µ¹SİѾͺͧN.f µt¹ǉƞ½NՕ2 οSҸĩƔǇ ManR/ClrB O
McmA Rýǉ?MҎǨΕR ³±¹j͹ͺAf%AQiIՕ µt¹SҍқbŦeӃ^4;gdҸĩƔǇS˶ЫĸȯRӳѵN.f%E;N µt¹SҾӉRԅ¿AfOÏɇ=gfϧ±·¥¹¹jɵ
ϱ?ՕEgdSΩƳbԿΑͲ4 µt¹jǃ`OAfŰοϧԲSҪŎRš\AȦԪjѾˊ?G%µt¹ҎǨ˅å½NS RNA-seq ѾˊceՕ µt¹ǉƞ½NΑͲAfɷǓϧ±·¥¹¹j՛οѷį?G%;gdӟêǇSΩƳ˗šWԿΑͲ˗jöѱ?Օ µt¹jŘº͙ϰ͈O?GƧƠNS
͹ХjѼǡ?G%ԿΑͲ˗R2/M µt¹ƧƠNS͹ХSÖӑ4ҍ`dgG 3 οRK/M cdtAՕcdtBՕ
cdtC OžŴ?G%cdtA O cdtB TEgFg µt¹±· ¹O?MƬź=gM/f Neurospora
crassa cdt-1 šW cdt-2 St³µzN.f% µt¹ƧƠNS͹Хï½4ҍ`dgGΩƳ˗TQ3JG
4ՕcdtA ΩƳ˗T±y¹NS͹Х4ï½?M/G%˹R ³±¹šW¦·¹͹ͺȾjғZGO;hՕ/BgR2/Ma CMC ´¹¼NSµSƷŎTѷdgQ3JG4Օv±y¦··NT cdtAՕ
cdtBՕcdtC SԿΑͲ˗Nµ4ɧƺ? cdtA ΩƳ˗NTЎǩ?G;O3dՕ;gd4¦·¹ΑͲҎǨͧҮSҍқbŦeӃ^Rԅ¿Af;O4ίƅ=gG%
ˀΧσT͹Χ ·¹'o¡¹¯·ŁįƨήΕΧσɷӑÐ˩(OӀˋ̒ͺΝ'Ӏˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩(Sʆɼjŧ9MѦigG%

Possible transporters involved in cellulase and hemicellulase expression in Aspergillus nidulans
Emi Kunitake, Kyoko Kanamaru, Makoto Kimura, Tetsuo Kobayashi

 69 —P-69
±·¥¹¹ʇƷRcf}pӯSƺӵ͹ͺñӴěʩŏǿ̠ɂ, ƺϘąº  ՒӶ̝ȀƺՓ)ΚΕ* }pӯTՊё(Aspergillus oryzae)N͹ͺ=gfÑ˹áҚͺͧN,µ¹̭ȾjԉǘAf;O
Rce©±·S͹ɐjɛĸAf%}pӯTƧƠÂRǪӵSΪӯ²p¨j̼ŅAfO,͹ͺ4ј?7ԉǘ=gf;O4΢dgM/f1)%E;NÜƓɑ&T,ՊёSΪӯ²p¨SŦeӃ^Rԅif±·¥¹¹jѷį?ՕESӟêǇjΩƳAf;ON}pӯS͹ͺϪSʇƷjΚɫ?G%)ʘ̥OϹˌ* Պё¹¡¹Âce,Ϊӯ²p¨SŦeӃ^Rԅif±·¥¹¹ӟêǇ(nrtA)jѷį?G%˹R,;SӟêǇSΩƳ˗jŦȮ?}pӯ͹ͺSȦԪSѾˊjѦJG%ESϹˌ, ∆nrtA˗TԿ͕ȑRΪӯ²p¨4ǉƞAf˅å½Na}pӯS͹ͺ4έҍ=gG%]G, ∆nrtA˗NT}pӯ͹ͺ˅å½N}pӯ͹ͺRԅifӟêǇ(kojiA,R,T)4,}·µ¹³˗Rǣ?MԿΑͲ?M/f;O4έҍ=gG%Ͳƞ,ʳQfҋϳQѾˊjӑ`M/fդ Terabayashi et al.: Fungal. Genet. Biol. (2010) 47, p953-61.

Over expression of kojic acid synthesis genes by the transporter modification
Motoaki Sano, Harue Kitagawa, Shinichi Ohashi

(KIT)

P-70
ՊёSr³~µ¹³͹űɐjĸȯAfҸĩƔǇ AtrR O SrbA S˶Ы2cWϳЩħǯƞѾˊ˂ǵнȋՕƺƭ˿ՕѕŞƺα 1ՕͼÂͷȃՕʗҝǫȜՕǿˀӑ 1ՕÓżŌË(ˈŏƺԍ¸Ӏ¸͹ͧͺ˩ŁɐՕ1 Œїƺ¸Οё·¹)ʜſѷɊˑΏO?MŐΐ¼̹ĺQƈ԰OQJM/fm¢³x³ΏSÄQŞƔёN.f Aspergillus
fumigatus RǣAfʸňQџľO?Mm¹³Ϫџľ4̕ͻ=gM/f4ՕϩͪёSίAџľƹľНȾ4ΟёΏ̠ΐSƺ5QԖǘOQJM/f%Պё A.oryzae 4ίAm¹³ϪџľНȾRT ABC ±·¥¹¹Sԅ
¿4Ïɇ=gՕ;gdӟêǇЖT Zn2Cys6 ƣҸĩƔǇ AtrR RcJMĸȯ=gM/f%]GՕ AfatrR ΩƳ˗S RNA-seq ѾˊRceՕAtrR T ABC ±·¥¹¹S^QdBՕbHLH ƣҸĩƔǇ SrbA ĸȯ½Sr³~
µ¹³͹űɐӮϰӟêǇЖSΑͲRaԅiJM/G%;SÐT AtrR O SrbA 4r³~µ¹³͹űɐϸҴjŖғΕRĸȯ?M/f;Ojίƅ?M2eՕESĸȯ˶ˬSѾʣjΚɫ?G% atrR/srbA ÑӳΩƳ˗jöɐ?Օm¹³ϪџľjŶ_ƧƠR2/M͹Х҉ԽjѦJGO;hՕÑӳΩƳ˗
T atrR ŘͫΩƳ˗OųϑSɊŧȾjί?G%;gceՕatrR Tr³~µ¹³͹űɐϸҴjΛɶΕRĸȯ?M/fūЫȾ4ίƅ=gG%˹RՕŰҸĩƔǇSÁʿϊR GFP jӐϹ=CG±§jˬϚ?ՕŰҸĩƔǇΩƳ˗RǨĢAf;ONϳЩħǯƞѾˊjѦJG%ESϹˌՕAtrR TˬɐΕR˘Rǯƞ?ՕSrbA T˘г/ǩЩóRǯƞ?M/G%ͲƞՕSrbA SϳЩħNSʳQfɭŊjѾˊÂN.f%

Functional and subcellular localization analyses of transcription factors, AtrR and SrbA, involved in ergosterol
biosynthesis in Aspergillus oryzae
Kohei Sugiyama, Ayumi Ohba, Daisuke Hagiwara1, Mizuki Tanaka, Takahiro Shintani, Susumu Kawamoto1, Katsuya
Gomi(Div. Biosci. Biotechnol. Future Bioind., Grad. Sch. Agric. Sci., Tohoku Univ., 1MMRC, Chiba Univ) 70 —P-71
Aspergillus nidulans S sirtuin moo¨RcfÑ˹áҚϪSΑͲĸȯèѠщӲǇՕ ъˀÚҼՕˠǭăÝՕ ԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓ sirtuin T·Яm ³ŎӮϰՒHDACՓy± RİԲ=gf NAD+ýǉΕ HDAC N.e͹ͧ΂RȎ7Ąǉ=gM/f%sirtuin T· H4 SЯm ³ŎjĂӑAf;ORcJMՕ µyµ¦·ˬӏSȢɐSĂӑOȡҊӟêǇS¹·o´··zjѦ0%ɑ&TՕϩͪёSª³͹ͧN.f Aspergillus
nidulans S sirtuin (SirA)4ՕNAD+ýǉΕR· H4K16 jЯm ³ŎAf;ORcJM²z¦·2cW¢²· G S͹űɐӟêǇΑͲOES͹ͺjɛĸAf;Ojѷį?G%?3?ՕSirA 4ĸȯAfßSÑ˹áҚϪb SirA âƸS sirtuin ·yҮS˶ЫRK/MT¾ʣN.f%ÜƓɑ&TՕDNA ¦oyµm´oѾˊRcJM SirA 4ѲʎSÑ˹áҚϪӟêǇSΑͲjɛĸ?M/f;
Ojѷį?G%=dRՕˀёS sirtuin ˭·yҮj}¹Af AN1226ՕAN1782ՕAN7461 2cW AN11873
S0IՕAN1782 2cW AN7461 RǣȺAfϷɺ1·yҮ4 sirtuin ̭ȾjʸAf;OjΑѷ?G%]GՕsirAՕAN1226Օ AN1782Օ AN7461 2cW AN11873 SӟêǇΩƳ˗Sёój HPLC RcJMѾˊ?GO;hՕŰӟêǇΩƳ˗TӴ͹˗O·QfáҚͺͧj͹ͺAf;O4ѷį=gG%;S0IՕsirAՕAN1782 2c
W AN11873 ӟêǇS˸ɽRcJM austinol 2cW dehydroaustinol S͹ͺӵ4ƱŅ?Օ;gdS͹űɐӟêǇSΑͲ4¼ʢ?M/G%;gdS;O3dՕaustinol 2cW dehydroaustinol T sirAՕAN1782 2cW AN11873
RcJMrqnyRĸȯ=gf;O4ʣd3OQJG%]GՕŰ sirtuin 4ȦԪj¿1fáҚͺͧ
4·QJM/G;O3dՕŰ sirtuin TEgFg·QfÑ˹áҚϪSӟêǇSΑͲjĸȯAfOЛ1dgG%
Aspergillus nidulans sirtuins regulate secondary metabolisms
Eriko Ito, Ryosuke shigemoto, Shunnsuke Masuo, and Naoki Takaya (Faculty of Life and Environmental Sciences,
Univ. of Tsukuba)

P-72
ՌՊё

²·ou³¤w¢¹ӟêǇR29fo·µ·̄ǉȾSѾˊΥͼď, ÆĄǺɂ, ˥ͼǠÛ, ļͼ̱, ǷˀЄǇ, όħӗԙ, ǵȢ̫ȋՒˈÙӀȀƺ¸Ⱥ͹θՓՌՊё Aspergillus oryzae S ²·ou³¤w¢¹ӟêǇ ocpG NTo·µ·̄ǉ4ұ
;eՕocpG ӟêǇÂRǉƞAf 3 KSo·µ·TEgFḡǉŀű4·Qf;OjºʨȌSˀ}·l´·NƬź?G 1)% ocpG ӟêǇSo·µ·SөĲOîГS/Bg34±o·z¹·RȦԪj¿1M/fS3ʣd3RAfG`RՕo·µ·өĲS^jĢgʵ1G ocpG ӟêǇjöѱ?EgFgS
o·µ·S±o·z¹·SƷŎj˧҂?G%
ocpG ӟêǇ˸ɽ˗j£O?MՕ ocpG ӟêǇSώ 1 o·µ·өĲOώ 2 o·µ·өĲSîГjĢgʵ1G˗jöѱ?G%;S˗jՕw¨§³yjƆºSφϰ͈O?G Czapek-Dox ̶óƧƠN 24 ʪԄƧԸ?ՕȮdgGёó3d mRNA jϦѱ?Օ cDNA űɐjѦQJG%ȮdgG cDNA jӺƣO?M
ocpG ͨ·Ε±o¦¹jͻ/M PCR jѦQ/Օ;gdS PCR ͺͧj±§RɰĢ?M±o±²¹
jöѱ?G%ĸԌӮϰĮʹ]GT PCR RcJM±o·z¹·jέҍ?G%Ӵ͹ƣS ocpG ӟê
ǇjaK˗RK/Maų˭SѾˊjѦQ/Օ±o·z¹·j̎Һ?G%ESϹˌՕ ocpG o·µ·Ģgʵ1˗TӴ͹ƣS ocpG ӟêǇOT·Qf±o·z¹·jί?G%ºоΕRo·µ·̄ǉ4͹@fѵƔO?MՕo·µ·өĲÂRǉƞAf±o·zz³OՕ mRNA SİǇħƯƨ
ǣRceȢɐ=gfÑ˹ˬӏ4Л1dgM/f4Օ ocpG o·µ·Ģgʵ1˗TƯƨөĲRýǉΕQ±o·z¹·jί=Q3JG%E;N ocpG S mRNA SÑ˹ˬӏjÏͅ?GϹˌՕÑ˹ˬӏÂR2
9f±o·zz³SîГSƷŎO±o·zŀűSƷŎOSԄRԅāȾ4ѷdgG%
Q2$ˀΧσSºӧT͹Χ ·¹ƨήɷӑÐ˩Sº͸O?MѦigGaSN.f%1) ΥͼdՕώ 12 ƓϩͪёİǇ͹ͧǋ}·l´· Ĥ͐ѵʞԛՕp.56
The intron retention analysis of serine-type carboxypeptidase gene in Aspergillus oryzae
Ken Ishida, Megumi Kuboshima, Hiroto Morita, Hiroshi Maeda, Ayako Okamoto, Michio Takeuchi, Youhei Yamagata(Dept. of Applied Biological Science, Tokyo Univ. of Agriculture and Technology) 71 —P-73
Aspergillus oryzae R29f 331-25 sense RNAՕ331-25 antisense RNA S˶ЫѾˊӂÔԚՕǁͼПՕόħӗԙՕǵȢ̫ȋ ՒˈÙӀȀƺ¸Ⱥ͹θՓ)ЧʭOΚΕ*ՌՊёSİ͹ǇšWΑцİ͹ǇS EST ѾˊSϹˌՕİ͹ǇS EST SÂNT 331-25 ӟêǇԮƦ3dҸĩ=gG antisense RNA ͽˆS EST 4ʶaƹ7Օ528 S0I 43 jŚ`M/G%ºʘՕӫԲІűΧσɕRcJMĤԃ=gM/f CAoGD (Comprehensive Aspergillus oryzae Genome Database) NTՕ331-25
ӟêǇԮƦ3dT sense RNA (SN RNA)Օantisense RNA (AS RNA) SÁʘ4Ҹĩ=gf;O4ί=gM/f%]GՕɑ&SâļSΧσR2/MՕǓӵ PCR Rcf SN RNA O AS RNA SǉƞӵS˧҂NՕAS RNA Tİ͹ǇRTǉƞAf4ՕΑцİ͹ǇՕёϩՕİ͹ǇΠ͹ΛļёóRTǉƞ?Q/;Ojʣd3R?G%]GՕSN RNA Tİ͹ǇOİ͹ǇΠ͹ΛļёóRǉƞ?Օд͒?Gİ͹ǇRTĖ3RѷdgՕёϩRTǉƞ?M/
Q/;Ojί?G%=dRՕ331-25 ӟêǇԮƦ˸ɽ˗R2/MՕİ͹ǇȢɐЫ4ï½Af;Ojέҍ?G(1)%ÜƓSΑѫNTՕSN RNA O AS RNA S˶Ыjʣd3RAfG`RՕ SN RNA ӖĿΑͲ˗ՕAS RNA ӖĿΑͲ˗SöѱjѦJGSNՕ;gRK/MƬźAf%)ʘ̥šWϹˌ*T@`RՕRIB40 ˗3dɢį?G RNA jͻ/MՕAS RNA S¹yr·ѾˊjѦJG%
ESϹˌՕAS RNA T 60 m§ӯ̄ƨâ¼S¢j}¹N5Q/;O4ʣd3OQJG%˹RՕSN
RNA ӖĿΑͲ˗jöѱ?ՕSN RNA S¹yr·ѾˊjѦJGϹˌՕSN RNA T 444 m§ӯ̄ƨS·yҮj}¹?M/f;O4ί=gG%]GՕSN RNA ӖĿΑͲ˗NT̑ÂёϩSìԁ4ѷdgBՕİ͹ǇȢɐЫ4ï½?M/f;O4ί=gG%ºʘՕAS RNA ӖĿΑͲ˗TՕѫͲȢRƷŎTѷdgQ3JG%ͲƞՕ=dRҋϳQѾˊjѦJM/f%(1) ӂÔd, ώ 13 ƓϩͪёİǇ͹ͧǋu·l´·ѵʞԛ p. 50 (2013)(2)
Analysis of 331-25 sense RNA, 331-25 antisense RNA in Aspergillus oryzae
Masaru Tsujii, Satoshi Okuda, Michio Takeuchi, Youhei Yamagata
Dept. of Applied Biological Science, Tokyo Univ. of Agriculture and Technology

P-74 (O-10)
Aspergillus aculeatus R29f dipeptidyl peptidase 4 S˶ЫѾˊӓÍИƼՕƛ˾ϾЕՕҝĆ̠Օ͙ҝԬºՕǿũĽů ՒԇȐƺԍ¸͹͸θՓɑ&TՕA. aculeatus T-DNA ɰĢƷ·˗±o±²¹3dŘԝ?G ³µ¹ҎǨЫ˸ɽ˗R2/MՕ
dipeptidyl peptidase 4 (dpp4) ӟêǇ4ΩƳ=gM/f;Ojѷ/H?G%A. aculeatus DPP4 T A. fumigatus šWƄÌԲS DPP4 OEgFg 67 %Օ31 %SΜųȾjʸ?M2eՕDPP4 T͹ͧR2/MȎ7Ąǉ=gM/fӮ
ϰN.f%ƄÌԲ DPP4 TՕ¢£³ª·S N ʿϊĐ3d 2 ΆΚS Pro ]GT Ala S C ʿϊĐjıʕA
f;ON˭&Qz³êӘjĸȯ?M/f%Aspergillus RTՕdpp ӟêǇ4 4 οǉƞAf4/BgSӮϰa͹ʹ˶ЫRԅAfƬźTQ/%E;Nɑ&TՕϩͪёR29f DPP4 S˶ЫjѾʣAf;OjΚΕO?MΧ
σjӑ`M/f%ʗGRöį?G dpp4 ΩƳ˗ (Δdpp4) R2/M cellobiohydrolase I ӟêǇϑSm ³b µt¹RceҎǨ=gfӟêǇSΑͲTՕҎǨĳʼRԌǓΕŔǪ?M/G%ºʘՕxylanase Ib ӟêǇϑSw±·bwµ¹RceҎǨ=gfӟêǇSΑͲӵTƷŎ?M/Q3JG;O3dՕDPP4 T ³µ¹ҎǨSĸȯRԅ¿?M/f;O4ί=gG%˹R}·µ¹³˗ՕΔdpp4Օdpp4 ԿΑͲ˗ (dpp4-OE) R29f DPP ̭Ⱦ
j Gly-Pro-pNA jƨҮRͻ/MͅǓ?GϹˌՕdpp4-OE R2/MʸɈR DPP ̭Ⱦ4¼ʢ?M/G%]GՕΔdpp4NT}·µ¹³˗O̎Һ?MёóΩΨȫSū͋Ⱦ΁İS̭ȾRTƺ5Qә/4Q3JG4Օёó̄̓S
Triton X-100 ū͋Ŏ΁İNTϬ 2/3 Rï½?M/f;O4ҍ`dgG%;S;O3dՕDPP4 4гRϹű?M/f;O4ɷͅ=gGG`ՕͲƞ DPP4 SǯƞѾˊjѦJM/f%]GՕΔdpp4Օdpp4-OE R29fȢҮSƷŎaͲƞѾˊÂN.f%
Functional analysis of dipeptidyl peptidase 4 in Aspergillus aculeatus
Syota Yuki, Emi Kunitake, Shuji Tani, Jun-ichi Sumitani, Takashi Kawaguchi(Grad. Sch. Life & Env. Sci., Osaka Pref. Univ.) 72 —P-75
Aspergillus oryzae Soµs¹·ЖS˶Ы2cWǯƞȾSѾˊʟǿуòѓ, ΥͼŒϾ, ǵǿϹ, Œáę, ÂǺʧϲ Ւʣ̠ƺԍ¸Ӏ¸ӀŎՓoµs¹·T,ϩͪё¸ɣǇёԲ4͹ͺAfϳЩѫǴ·yҮN.f%ïİǇӵ(70~150 a.a.)SÁѻǆȾ·yҮN.e,̑ÂSёϩbİ͹ǇSѫǴRзȃԛű?MŘǴjȢɐ?,ёóRʂ̒Ⱦjà¿A
f%՘KSё˗TΜųȾSï/oµs¹·ӟêǇjѲʎʸ?M/f4,ESù/İ9RK/MT[OkPѾʣ=gM/Q/%
ϐМdT Aspergillus oryzae Soµs¹· HypA/RolA, B, C SΑͲOǯƞȾRK/M˧҂?,HypA
TÄO?Mİ͹ǇR,HypB TёϩRǯƞ?,HypC TӍȉS˅å½NTΑͲӵ4ǪQ/;OjѼǡ?M/f%=dR,hypA O hypB Sµª¹¹j×ɺ?Gʪ,HypA O HypB SǯƞӧîaĢgʵif;OjѼǡ?,HypA
O HypB SǯƞȾTŰ&Sµª¹¹RýǉAf;Ojʣd3R?M/f%İ͹ǇRǯƞAfoµs¹·T HypA H9N.f;O3d,ˀΧσNTESİ͹Ǉͨ·ΕQΑͲ˶ˬjѾˊAfG`,̆ԓΕR˸
ƿ=CG hypA µª¹¹RѣĞ·yҮӟêǇjӐϹ?,A. oryzae RǨĢ?G%ESϹˌ,İ͹Ǉͨ·ΕΑͲRǜ¿AfԮƦ4 hypA ORF ¼̮(-1200գ-400)2cW(-280~-200)ԮƦRͫχ?MǉƞAf;Ojѷį?
G%(-280~-200)ԮƦħRT,İ͹ǇȢɐjĸȯAfҸĩƔǇ AbaA SɷǓϹűԮƦ(ARE)4 3 Kǉƞ?,hypA S
İ͹Ǉͨ·ΕΑͲOSԅ¿4Ƞ7ίƅ=gG;O3d,;S 3 KS ARE j˸ƿ=CGO;h,İ͹Ǉͨ·ΕΑ
Ͳ4̵ƿ?,ARE 4 hypA Sİ͹Ǉͨ·ΕΑͲRӳѵN.f;Ojʣd3R?G%
Characterization and localization of hydrophobins in Aspergillus oryzae
Fuyuka Hayakawa, Chie Ishida, Yui Yamakawa,Yu Chiyo, Harushi Nakajima(Dept. of Agricultural Chemistry, Univ. of Meiji)

P-76 (O-7)įцӮ̋եϩͪёNS˦ͧ-ΟёѤű·w¹S˶ЫΜѰOr´·ȺϓÂǵΟͽЕ 1,2ՕŪǿďƼӦ 3, ŲѷƉ 1, ԊӧʍɄ 1,2(1 ˈŏƺ¸ʾˆΧ, 2 ˈŏƺ¸ԍӀ¸͹ͧͺ˩Łɐ, 3 Univ. of Gothenburg, Dept. of Chemistry and Molecular BiologyՓ ˦ͧSµoR2/MՕr´· ·¹O?M˶ЫAf AtETR1 T·w¹(HK)̭
ȾjɪIՕr´·RcJMES HK ̭Ⱦ4ĸȯ=gf%ˀΧσNTՕ;S˦ͧͽˆSr´·Ϲű©o·OӮ̋ƆºS HK N.f ScSln1p 2cWӮ̋NS HK ˶ЫΜѰ4ҍ`dgM/fϩͪё HK S AnTcsB RŅ
1Օ̴ӋƝɊŧRԅāAf AnNikA S·w¹©o·OѤű?G HK jEgFg҅ҁ?Օr´·ȺϓȾS HK R˶ЫʇƷ?GİǇSӏɐj҉^ՕӮ̋¸ϩͪёNS HK ˶ЫΜѰȾOr´·ȺϓȾR
K/M˧҇?G%;g]NRįцӮ̋ Sln1p ̈́ȑɊŧȾ˗R2/M ScSln1p S˶ЫΜѰȾj҈þ?GϹˌՕ
ScSln1p 2cW AnTcsB SѤű HK 4 ScSln1p S HK ̭ȾjΜѰAf;Ojέҍ?G%]GՕѤű HK jǨĢ?G˗NTr´·ĮʹN͹ХSɛĸO HOG ϸҴSĸȯ4ҍ`dgG;OceՕr´·ȺϓȾjέҍ?G%
Ņ1MՕAnNikA SѤű HK RK/Maų˭R HK ˶ЫΜѰȾOr´·ȺϓȾjέҍ?Օ̴ӋƝĹ͔SɊŧRӳѵO=gf HAMP ©o·S˶Ы4Ѥű AnNikA RЂɪ=gM/f;Ojέҍ?G%ͲƞՕįцӮ̋R
2/M HK ˶ЫΜѰȾjέҍ?GѤű HK RK/MϩͪёNSΑͲϪjˬϚ?ՕѾˊjӑ`M/f%(ˀΧσTՕ͹Χ ·¹o¡¹¯·ŁįƨήΕΧσɷӑÐ˩OӀˋ̒ͺ˩¸Գƀͺ˩θǋəѧΧσɷӑÐ˩Sʆɼjŧ9MѦigGaSN.f%)
Functional complementation and ethylene response of plant-fungal fusion histidine kinase in budding yeast andfilamentous fungi.
Mayumi Nakayama1,2, Kentaro Furukawa3, Akira Yoshimi1, Keietsu Abe1,2(1NICHe., Tohoku Univ., 2Grad. Sch. Agric. Sci., Tohoku, Univ., 3 Univ. of Gothenburg) 73 —P-77
Fusarium graminearum 2cW Fusarium sporotrichioides R29fҸĩƔǇ TRI6 S˶ЫÒɺȾÂǾòºՕļͼºѦՕӶÃÙǇՕǩˋƃƽՕʽ˄Ο ՒŴƺԍ¸͹žӀՓFusarium graminearum TÑ˹áҚRceo B ²} ·j͹ͺ?ՕFusarium sporotrichioides To A ²} ·j͹ͺAf%ÁМT²} ·͹űɐy±¹jʸ?M2eՕ;S̭ȾŎRTy±¹ħҸĩƔǇ Tri6 4ÂȶΕQȧŀjɣ0%;;RՕF. graminearum Tyµ¹j͙ϰ͈O?GƧƠ (YSƧƠ)NT²} ·j͹ͺAf4Օz³}¹j͙ϰ͈O?GƧƠ (YG ƧƠ)R2/MT²} ·j[OkPͺ͹?Q/ºʘN F. sporotrichioides T YS, YG ƧƠS/BgR2/Ma²} ·jԿ͹ͺAf
O/JGͨȴjaK%2 οԄNS;Sc0Qә/j͹^įAѵƔRԅ?M΢ѷjȮfG`ՕˀΧσNT Tri6ӟêǇͺͧS˶ЫSȂ·b Tri6 ҸĩҎǨSә/R͚͝jϺeѾˊjѦJG%]BՕF. gramonearum R2/M FgTri6 j FsTri6 R¶?G˗jöѱ?Օ²} ·͹ͺȾbϸҴӮϰSҸĩҎǨjѾˊ?G%]GՕF. graminearum T YG ƧԸ˅å½R2/M Tri6 SҸĩ4[OkP͹@M/
Q/;O3d 2 οԄS YG ƧԸ˅åNS²} ·͹ͺȾSә/T Tri6 SҸĩҎǨЫRұƔAfOɷǓ?Օ
F. graminearum R2/M FgTri6 ]GT FsTri6 jˬɐΕRӖĿΑͲ=CG˗jöѱ?ՕYG ƧԸ˅åNS²} ·͹ͺȾQdWRϸҴӮϰӟêǇSҸĩ̢ͪSѾˊjѦJG%;gdSϹˌjX]1Օ2 οԄR29
f TRI6 S˶ЫÒɺȾb Tri6 ҸĩҎǨЫS²} ·͹ͺĸȯYSȦԪjƬźAf%ˀΧσSºӧT͹Χ ·¹Sʆɼjŧ9ѦigG%
Functional compatibility of Transcription factor TRI6 between Fusarium graminearum and Fusarium
sporotrichioides.
Yuichi Nakajima, Kazuyuki Maeda, Kyoko Kanamaru, Tetsuo Kobayashi, Makoto Kimura(Nagoya Univ. )
P-78
ϩͪё Trichoderma reesei R29f pH ýǉΕ

³±¹͹ͺ©u¨SѾˊȋ̝ƺ˴ՕƯǱȍ˴Օȹͼ̫ÝՕǩύŞ̿ՒԁǷəθƺ¸͹ͧՓϩͪё Trichoderma reesei TՕ ³±¹Կ͹ͺёO?M΢dgM/f%;g]NRυ͞Ʒ·ǨĢRce
ʳQfԿ͹ͺƷ·˗4ŦȮ=gՕʜˀR2/MaÀ΂Ε˰͉˗ QM9414 ˗ceԿ͹ͺƷ·˗ PC-3-7 ˗4ŦȮ
=gM/f%Ͳƞ]NRԿ͹ͺRǜ¿AfѵƔSͨǓRŵ9Օ˭&Q˅åRǣAf ³±¹͹ͺȾjѼǡ
?G%ESÂNՕ͸ư pH RǣAf ³±¹͹ͺȺϓj҈þ?GϹˌՕQM9414 ˗NT pH 4ƱŅAfRK
gMՕ ³±¹͹ͺȾ4́Ǫ?M/GSRǣ?ՕPC-3-7 ˗NTiB3RƱŅ?M/G%ϩͪёTՕpH z³êӘ˶ˬjĄɪ?M2eՕPal ·yҮЖRce pH ȺϓҸĩғϙƔǇ PacC 4̭ȾŎ=gՕ˭&QӟêǇSΑͲĸȯjѦJM/f;O4Ƭź=gM/f%ˀΧσNTՕT. reesei R29f pH ýǉΕ ³±¹͹ͺ©u¨SѾʣj҉^G%
T. reesei R2/MaՕPal ·yҮЖ2cW PacC £ªµz4ǉƞ?Օ̎Һ|¨Ѿˊ3d;gdSӟêǇRƷ·4ĢJM/Q/;Ojέҍ?G%ESG`ՕÁ˗R2/Mų˭R pH z³êӘ˶ˬ4öͻ?M
2eՕ ³±¹͹ͺȾSә/T PacC RceΛɶΕNTQ7ՕԄɶΕQĸȯN.f;O4ίƅ=gG%E;
NՕPacC ΩƳ˗jˬϚ?GϹˌՕQMpacC ˗R2/MՕԿ pH ĐNS ³±¹͹ͺȾ4ƱŅ?G%;S;O3dՕPacC Rceғϙ=gfôd3SƔǇSǉƞ4Ƞ7ίƅ=gG%=dRՕ¦oyµm´oѾˊSϹˌ3dՕƷ·˗ԄN ³±¹͹ͺRȷԭQҸĩғϙƔǇ xyr1 2cW ³±¹ե § ³±¹ӟêǇ4·QfҸĩĕŵN.f;O4έҍ=gG%â¼S;OceՕԿ pH ĐR2/M PacC RcJMғϙ=gfôd
3SƔǇRceҸĩғϙƔǇ xyr1 4ɛĸ=gՕ ³±¹͹ͺ4́ǪAf;O4ίƅ=gG%ͲƞՕʜˀƣϪϽ˴Ʒ·˗R29f pH ȺϓȾRK/MѾˊ?Օ ³±¹͹ͺɛĸƔǇSͨǓj҉^M/f%
Analysis of the pH-dependent cellulase production mechanism in filamentous fungus Trichoderma reesei
Hiroki HirasawaՕKoki ShioyaՕYosuke ShidaՕWataru Ogasawara (Dept. of Bioeng.ՕNagaoka Univ. of Tech.) 74 —P-79ϩͪё Trichoderma reesei S³±¹͹ͺĸȯƔǇSЃДΕѾˊéͼǐ˴ՕƯǱȍ˴Օȹͼ̫ÝՕǩύŞ̿ ՒԁǷəθƺ¸͹ͧՓϩͪё Trichoderma reesei T ³±¹¸ § ³±¹SԿ͹ͺёO?MՕÀ΂ÂNȀ˩ΕRĶͻ=gM/f%ͲƞՕT. reesei S ³±¹¸ § ³±¹͹ͺ˶ˬSѾʣRŵ9GΧσ4ӑ`dgM2eՕ;g]NSΧσN/7K3SҸĩғϙƔǇS˶Ы4ųǓ=gG4Օĸȯ˶ˬSģǚѾʣRTиJM/Q/%ºʘՕΧσ4ĝѦ?M/fϩͪёS Aspergillus ǳb Neurospora ǳQPNTՕƹοSҸĩғϙƔǇS˶Ы4Ѿʣ=g
M5G%;gdSΧσRceՕT. reesei S ³±¹¸ § ³±¹͹ͺ˶ˬaՕƹοƹ˭QҸĩғϙƔǇRceѲԜRĸȯ=gM/f;O4ίƅ=gM/f%E;NˀΧσNTՕT. reesei R29f Aspergillus ǳb
Neurospora ǳSʛ΢ҸĩғϙƔǇt³µzS˶ЫѾˊjѦ/Օ ³±¹¸ § ³±¹͹ͺĸȯ˶ˬSģǚѾʣjΚΕO?G%
Aspergillus ǳb Neurospora ǳSʛ΢ҸĩƔǇSt³µzɵϱSϹˌՕT. reesei S|¨ÂRՕ42 ĈSɷǓҸĩĸȯƔǇӟêǇjΑѷ?G%ES0IՕ ³±¹͹ͺYԅ¿AfOȼigf 15 ĈSɷǓҸĩғϙƔ
ǇӟêǇjӞɞ?ՕT. reesei QM9414 ˗SŰӟêǇΩƳ˗SˬϚjѦJG%]BTՕ ³±¹͹ͺYȠ7ԅ
¿AfOЛ1dgfɷǓ͙ϰ͈·ŎɛĸĸȯƔǇRΠΚ?M˶ЫѾˊjѦJG%ESÂNՕɷǓЯ®w·ŎӮϰ cre2 SΩƳ˗NTՕz³}¹ǉƞ½Na ³±¹͹ͺȾjίA;Ojέҍ?G%ͲƞՕɷǓҸĩғϙƔǇΩƳ˗jͻ/G ³±¹͹ͺȾS҈þ2cW T. reesei R29ft³µzS˶ЫѾʣjѦJM/f%
Global analysis of cellulase production regulators in filamentous fungi Trichoderma reesei
Hiroki Aita, Koki Shioya, Yosuke Shida, Wataru Ogasawara(Dept. of bioeng., Nagaoka Univ. of Tech.)P-80oθ˦ͧ/aIΎёS Argonaute3 T RNA o´··zjҡRĸȯAf
Ģҝȥщ, ˲Ρ÷ǀ, ÂǱʐƢ Ւβɓƺԍ¸ӀՓRNA o´··zTзȃS|¨jpo³b±·¥·O/JGƸˆȾSƔǇ3dԈȯAfȧŀjɣ0Ο˘͹ͧģоRĄǉ=gM/f˶ˬN.f%oθ˦ͧ/aIΎё(Magnaporthe oryzae)Ra;S˶
ˬ4ǉƞAf4, ˀΧσǖNTųё|¨ÂRǉƞAf RNA o´··zԅӐӟêǇSΩƳ˗4ЃДΕRöѱ=gM/f%ˀΧσNTª³͹ͧN.fmu·uR£ªµz4ǉƞCB, ES˶Ы4ʾ΢Q
Argonaute3(Ago3)jѾˊ?G%
Ago3 jozµ¦o·НȾӟêǇ(Hph)NГɺ?Möѱ?GΩƳ˗R Hph j¹|O?G 2 οԲSo´··z}·±y(pSilent-Hyg, pMGY70-Hyg)jEgFgǨĢ?G%pSilent-Hyg T m· RNASͺ͹Rce RNA o´··zjҎǨ?, pMGY70-Hyg NT LTR ´µ±·¥· MAGGY R HphөĲSºӧjϷ^Ӄ_;ON±·¥·OųʪR Hph 4o´··z=gf;O4ʼȩ=gf%ES
Ϲˌ, }·µ¹³N.fo¹(MoDCL2)ΩƳ˗NT WT ˗O̎Һ?Mo´··zňͯ4ԱјRï½?GSRǣ?, Ago3 ΩƳ˗R2/MT, ͨR pSilent-Hyg Rcfo´··zňͯ4ƺ57¼ʢ?G%?3? MAGGY SҸλԯȑb©³ŎͯRT Ago3 ΩƳ˗OӴ͹˗Nƺ5Qә/Tҍ`dgQ3JG%â¼S;
O3d Ago3 T dsRNA RceҎǨ=gf RNA o´··zjɛĸΕRĸȯ?M/f;O4ίƅ=gG%
Argonaute3 negatively regulates RNA silencing in Magnaporthe oryzae
Akihide Iritani, Kana Yokoya, Hitoshi Nakayashiki(Grad. Sch. Agr. Kobe Univ.) 75 —P-81
ХοYSȺͻjΚΕO?Go{|¨өĲʏĒơˀѯº, ñѠȹρՕӶǇΟË 1Օ̯Ӵ=O^ 1ՕǗǼǍǥ 2ՕΓΥӑ 3ՕǗǼſȜ 2ՒǸɗ͹ȀΧ, 1 ˈȀƺ¸͹žʹȀ, 2 ˥ˋІΧՕ3 Êƺ¸ӀǋΧσԍՓХοRĶͻūЫQȢNo{|¨өĲjʏĒAfÐjΚΕO?MՕde novo m ·³jѦ0OOa
RՕm ·³=gG contig jՕʛǉSӐӾƠƘYǣȺà9G%o{º˘ёϩóN.f G408PP-4 ˗ce|¨ DNA jɢį?ՕIllumina ΰS Hi-seq2500 šW GAIIx jͻ/M¢mr·̥šW©o¢m̥Rce
¹yr·jѦ0OOaRՕpacbio Rcfµ·z²¹S¹yr·jѦJG%de novo m ·³R
TՕclc genomics workbench jͻ/Օ©o¢m²¹šW pacbio ²¹jͻ/G scaffold ŎRT SSPACE šW PBJelly jͻ/G%]GՕo{SŰϷБ3d RNA jɢį?M RNA-seq jѦ/ՕG408PP-4 |¨өĲRǣ?M¦·zȫՕAugustus RceӟêǇÏͅjѦJG%G408PP-4 O D703P-9 S±|¨өĲO̎ҺAfÐN Allele-specific primer j҅ҁ?ՕӐӾѾˊjѦ0ÐNՕŰ contig jӐӾƠƘ¼RǣȺ=CG%¢
mr·±o±²¹ceȮGІƯƨԁϬ 4.6Gbp S¹yr·²¹jͻ/M de novo m ·³j
ѦJGO;hՕcontig ʎ=4,731ՕN50=36kb OQJG%©o¢m²¹ՕšW pacbio ²¹jͻ/M scaffold
ŎjѦJGO;hՕscaffold ʎ=1,963ՕN50=102kbՕІƯƨԁ 39Mbp OQeՕрǂQ N50 ċjȮfÐ4įˆG%|¨өĲšW RNA-seq ¹jͻ/MՕӟêǇÏͅjѦJGϹˌՕϬ 13,000 ӟêǇ4Ïͅ=gG%;g]
N 257 ӟêǇȒRK/M¦·zjѦ/Օ¦·z=gG scaffold SІƯƨԁT 32Mbp OQeՕscaffoldSІƯƨԁSϬ 8 ŀju¹N5G%
De novo genome sequence of Lentinula edodes for molecular breeding strategies
Yuichi Skamoto, Shiho Sato, Shinya Kaneko1, Satomi Asano1, Yasumasa Miyazaki2, Susumu Shiraish3, Kazuhiro
Miyazaki2(IBRC; 1Life Sci., Tokyo Inst. Tech.; 2 For. For. Prod. Res. Inst.; 3Grad. School of Agr., Kyushu Uni.)

P-82©µ³¢o terretonin ͹űɐ˶ˬSѾʣ2cWԅӐĆԷӮϰЖS˶ЫѾˊǸ̀ƺҽՕˉͼûƺՕ̸ǿǊЗՕԊӧӥʺ Ւˈƺԍ¸џՓϩͪё Aspergillus terreus S͹ͺAf terretonin T¥²{oO farnesyl ƨͽˆS³¢o3dQfͨ
·Qo²ƣŎűͧ (©µ³¢o) N.f%ANRģ 10 ӟêǇ3dQf terretonin ͹űɐӟêǇ
y±¹4 A. terreus NIH2624 ˗S|¨¹¡¹3dųǓ=gM2eՕES͹űɐϸҴRK/MTӟêǇΩƳb͹űɐӮϰS·οΑͲQPRceƺӧİ4ʣd3R=gM/f%?3?Q4dՕterretonin ͹űɐYSԅ¿4Ĵʣ?M/fӮϰЖS0IՕTrt6 (P450)ՕTrt7 (non-heme iron-dependent dioxygenase)ՕTrt14(hypothetical protein) S 3 KSӮϰRK/MTՕESѿǆ˶Ы4ʾHѾʣ=gM/Q/%ɑ&TՕterretonin͹űɐR2/MͨȴΕQŤȺN.f͸ɧƺŤȺjŶ_ĆԷŤȺj;gdSӮϰ4ɣ0OЛ1ՕES©u¨QdWR terretonin ͹űɐ˶ˬSģǚѾʣjΚɫ?G%
Terretonin ͹űɐӟêǇy±¹ÂRŶ]gfģ 10 ӟêǇj·οϩͪё Aspergillus oryzae RǨĢ?Օ͹űɐϪSĨˬϚj҉^GO;hՕterretonin 2cWESļԼóN.f terretonin A jȮG%Q2Օtrt14 jŶ]Q/ 9 ӟêǇΑͲϪT terretonin S©³r³ƨ4˸ƿ?G terretonin C 2cWESļԼój¿1f;O4Ĵ
ʣ?G%10 ӟêǇΑͲϪN terretonin 4͹ͺ=gG;O3dՕ;gdSӟêǇЖT terretonin j͹ͺAfSRȷѵőİN.fOЛ1dgf%]GՕTrt14 SΑͲSʸ͜Rce©³r³ƨSʸ͜4ƷŎ?G;O3dՕ
Trt14 T;S©³r³ƨSȢɐRԅ¿?M/f;O4ίƅ=gG%ͲƞՕTrt6ՕTrt7ՕTrt14 SҋϳQ˶ЫѾˊj in vivo QdWR in vitro NѦJM2eՕESϹˌRK/MaøCMƬź?G/%
Biosynthetic Studies on a fungal meroterpenoid terretonin and functional analyses of the tailoring enzymes
Taiki Iwabuchi, Yudai Matsuda, Takayoshi Awakawa, Ikuro Abe(Graduate School of Pharmaceutical Sciences, Univ. of Tokyo) 76 —P-83 (O-16)©µ³¢o anditomin ͹űɐSģǚѾʣˉͼûƺՕ̸ǿǊЗՕЭˀʋȍՕԊӧӥʺ Ւˈƺԍ¸џՓ©µ³¢oOTՕ³¢oSӧİˬӏjʸAfŎűͧSІκN.eՕϩͪё3dTˬӏƹ˭Ⱦ
QdWR͹̭ͧȾRǞ_ƹʎS©µ³¢o4Ƭź=gM/f%Aspergillus variecolor Sͺ͹Afanditomin TՕͨ·QİǇħˏ˵ˬӏjʸ?M2eՕES͹űɐSİǇƨΙRкż4ɪGgf%ɑ&TՕʨȌȑSˀéRM anditomin ͹űɐӟêǇy±¹SųǓjƬź?G%;g]NRՕ͹űɐĳʼ̆ԓjɣ0 5 K
SӮϰS˶ЫѾˊjѦ/ՕÓ͸ȾSİǇԾ˚jʸAf͹űɐÂԄóՒŎűͧ 1ՓSŘԝRɐń?M/f%Ü
ƓʗGRՕˀӟêǇy±¹S}¹Af 7 KSĆԷӮϰS˶ЫѾˊjѦ/Օanditomin ͹űɐSİǇƨΙѾʣjΚɫ?G%Ŏűͧ 1 âԋS͹űɐϸҴjÏͅAf;OTƖԞN.JGG`Օ·οϩͪё Aspergillus oryzae RMο&SϷ^űiCSĆԷӮϰΑͲϪjˬϚ?ՕȮdgGȢҮҸɺóR 1 jɜ¿ȫՕESáҚͧjİˊAf;ONՕŰĆԷӮϰS˶ЫQdWR͹űɐϸҴjɷǓ?G%Ű͹űɐÂԄóSŘԝՕˬӏ̙ǓR.GJMTՕŎűͧ
1 SűɐRԅif 5 KSӟêǇaűiCMΑͲAfϪjԬ˹ˬϚ?G%Ņ1MՕºӧӮϰRK/MTƺбёRMƺӵΑͲՕϦѱȫ in vitro S҉ԽRü?G%â¼RceՕanditomin Sģ͹űɐϸҴSѾʣRɐń?G%ˀ͹űɐR2/MTՕFe(II)2cW α-{z³³ӯýǉƣtw|¹ AndA 4Ñ̆ԓSŤȺjѿǆ?Օ
ͨ·Q bicyclo[2.2.2]octane Ծ˚Ȣɐjɣ0;O4Ĵʣ?G%]GՕ͹űɐSʶ϶̆ԓNTՕbTetw|¹N.f AndF 4ӯŎΕҸîŤȺRce anditomin SİǇԾ˚j¿1f;Ojѷį?G%
Complete biosynthetic pathway of fungal meroterpenoid anditomin
Yudai Matsuda, Takayoshi Awakawa, Toshiyuki Wakimoto, Ikuro Abe(Graduate School of Pharmaceutical Sciences, Univ. of Tokyo)

P-84
Emericella variecolor ͽˆʗѸ©µ³¢o͹űɐӟêǇy±¹S˶ЫѾˊģʰɹՕˉͼûƺՕ»˵ԒωՕԊӧӥʺ Ւˈƺԍџ¸ƻͧ͞ŎǋՓ©µ³¢oOT³¢oSӧİˬӏjʸAfŎűͧSІκN.eՕϩͪё3dTˬӏƹ˭ȾQ
dWR͹̭ͧȾRǞ_ƹʎS©µ³¢o4Ƭź=gM/f%ÂNaՕ3,5-dimethylorsellinic acidՒDMOAՓjұ͈OAf©µ³¢oRTՕOei9ƹ˭QİǇԾ˚4ѷdgf%Andrastin A TՕDMOA RͽˆA
f protein farnesyltransferase ԉǘľN.f4Օɑ&TANR Penicillum chrysogenum Wisconsin 54-1244 ˗S|¨¹¡¹ÂRȡҊŎűͧS͹űɐӟêǇy±¹Ւadr y±¹Փjѷį?ՕES͹űɐSģǚѾ
ʣRɐń?M/f%ÜƓՕȡΧσǖN±|¨¹{·ѾˊjǕʙ?Gϩͪё Emericella variecolor
S|¨ÂR adr y±¹OԲí?GӟêǇy±¹jѷį?GG`ՕES˶ЫѾˊRΠɗ?G%
ˀӟêǇy±¹RTՕandrastin A ͹űɐRԅifOɷǓ=gfӟêǇЖRŅ1MՕadr y±¹Â
SӟêǇOTԲíȾSï/ӟêǇ4 3 Kǉƞ?M2eՕ;gd4}¹AfӮϰЖRcJM andrastin A 4=dRĆԷ=gGŎűͧYOƷɺ=gf;O4ʼȩ=gG%E;NՕ;gd 3 ӟêǇS˶ЫѾˊjѦ0Z7Օ
andrastin A ͹űɐӟêǇЖOOaRϩͪё Aspergillus oryzae R2/M·οΑͲϪjˬϚ?G%ȮdgGȢҮҸɺójҎǨƧԸȫՕƧԸ¼̽ɢįͧj HPLC QdWR LC-MS İˊRü?GO;hՕʗGRİǇӵ4 14 Ʊ
Ņ?GŎűͧS͹ɐjέҍ?G%ͲƞՕˀŎűͧSˬӏ̙ǓQdWRŰӮϰӟêǇSҋϳQ˶ЫѾˊjѦJ
M2eՕESϹˌRK/MaűiCMƬź?G/%

Functional Analysis of a novel meroterpenoid biosynthesis gene cluster from Emericella variecolor
Zhiyang Quan, Yudai Matsuda, Takaaki Mitsuhashi, Ikuro Abe(Dept. of Natural Products Chemistry, Univ. of Tokyo) 77 —P-85
Penicillium purpurogenum R29f Monascus сϰ͹űɐԅӐ¥²{͹űɐӟêǇ
SɵϱяŞ̺ՕǩǾ̷ՕъʽЕ˴ՕՎѠÚՕʗǰӸȋՕŅѠԬՕʧѷԒʑ Ւʜƺ¸͹ͧҪ͈¸͹žŎǋՓ
ɑ&TՕˈmmRMΑӮȲ͹ͧO?MĶͻ=gM5GǇS0ё Monascus O¾ǎģǇS0ё PenicilliumS͹ͺAfĥӍ?GÑ˹áҚͺͧRK/MѾˊ?M/f%¾ǎģё Penicillium SʸȾÀáT˹ώRʣd3R=gKK.f4ՕPenicillium OǇS0ё Monascus SԄS͹̅ÀáOáҚͺͧ͹űɐӟêǇS̒ȋêʃOSԅӐȾT¾ʣN.f%E;NՕˀΧσNT Penicillium purpurogenum R29f Monascus сϰųʚó͹űɐRԅ
Ӑ?GӟêǇjͨǓAfG`RՕPenicillium purpurogenum SaK¥²{͹űɐӟêǇj˧ϱ?Օ
AspergillusՕMonascusՕPenicilliumՕTalaromyces ϑßSϩͪёͽˆ¥²{͹űɐӟêǇOS̎Һ2cW
©o·ˬӏSϪϽѾˊjѦJG%ȡΧσǖR2/MѾˊ?G Penicillium purpurogenum S|¨±¹
yr·jͻ/M Aspergillus, Penicillium ϑSϩͪё3dѷį=gM/fʛ΢S¥²{űɐԅӐӟêǇSƯƨөĲɆƬjƨRՕlocal BLAST search Rce˧ϱ?G%ESϹˌՕ26 ĈS¥²{ӟêǇSǉƞjέҍ
?G%=dRՕέҍN5G©o·ˬӏS0I KS ©o·jǣҠRİǇϪϽѾˊjѦJG%;SϹˌՕ
PKS/NRPS o²ƣՕLovastatin nonaketide synthaseՕconidial yellow pigment biosynthesis PKS ϑOΜųȾSԿ/՜z³¹SͨȴΕQ¥²{͹űɐӟêǇSǉƞjέҍ?G%ˀϩͪёͽˆ Monascus сϰųʚóRͨȴΕQ n-octanoyl ƨՕisoquinoline Ծ˚ˬӏ3d¥²{͹űɐӟêǇSϺeӃ^jѦJG%ͲƞՕ;SӟêǇS˶ЫjΜųϷɺ1Rceέҍ?M/f%

The search of Monascus pigment biosynthesis polyketide synthases gene in Penicillium purpurogenum.
Jun Ogihara, Ryo Kojima, Yoshiki Motegi, Ryo Saito, Teppei Arai, Jun Kato and Takafumi Kasumi (Dept. of Chem.
Life Science, Nihon Univ. )P-86 (O-17)
ϩͪё Aspergillus nidulans RcfƜƴ§·ӯSˬӏƷŎÂ͓ǀЕՕК̡ΧºՕԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓƜƴRҟǞRŶ]gf§·ӯT, ˦ͧ²z·ϑRͽˆAfхԺ͸bЬФʚӾjƹ7Ŷ_ԞİѾȾSԿ
İǇŎűͧN.eՕз͞΂NT͹ͧΕ]GTԥ͹ͧΕRİѾ=gf;ORcJMƠͳ¼S͙ϰȱ͸SЂɪRҢͬ?M/f%?3?Q4dՕºӧSϳёbΓсаˁёjԎ/GёԲO§·ӯOSΜÒöͻRK/MT[
OkPʾѾʣN.f%ˀΧσǖNTՕ;g]NRՕ Aspergillus nidulans S DNA ¦oyµm´oѾˊ3dՕ§·ӯS̼ŅRcJMˀёSѲʎSӯŎӮϰӟêǇSΑͲ4¼ʢAf;Ojѷį?M5GՒ2013 ȑՕˀ}·l´·Αѫ P-22Փ%
E;NՕˀΧσNTՕ A. nidulans SƧԸRë0§·ӯSˬӏƷŎSѾˊj҉^G%A. nidulans TƧԸR
ëJMƧƠÂS§·ӯjŷΠ?G%ёRŷΠ?G§·ӯOƧԸ̶ÂS§·ӯjEgFgƓť?Օ¹²rƷɺƣүƸİĞѾˊՒFTIRՓjѦJGO;hՕPIdaЬФʚՕm²³r¹³Օq¹³SƱŅ4
Ѽǡ=gG%ƧԸȫSƧԸ̶ÂS§·ӯSƙó 13C NMR ceՕu³¤wƨO©wƨSƱŅ4ՕԠîȂ͏ǓRcfǑЫƨİˊceՕu³¤·ӯOq¹³SŶӵ4ƱŅAf;O4ί=gG%]GՕ|³hӖİˊRceՕƧԸRëJM§·ӯ4ԿİǇŎAf;O4ʣd3OQJG%â¼S;O3dՕ§·ӯTΑͲҎǨ=gG A. nidulans SӯŎӮϰЖSė5RcJMӯŎӳű=gM/fOЛ1dgG%§·ӯS̼ŅRcJMԱјRҎǨ=gf Flavin-containing monooxygenase (AN10582)SӟêǇΩƳ˗jöѱ?MƧԸȫS§·ӯS FTIR ѾˊjѦJG4ՕǑЫƨSƷŎTӴ͹ƣ˗OƷidQ3JG%ͲƞՕ§·ӯSӯŎRԅifӟêǇSͨǓj҉^M/f%
Structural changes of soil humic acid by the fungus Aspergillus nidulans
Nami Nakazawa, Ken-Ichi Oinuma, Naoki Takaya(Faculty of Life and Environmental Sciences, Univ. of Tsukuba) 78 —P-87
ozµ¦o· B ĮʹRcf³±yr·͹ͺϩͪё Fusarium sp. RK97-94 R2
9fÑ˹áҚͺͧ͹ͺҎǨŅѠИ 1,2, ˀǵԿȍ 1,3ՕӽćԿȹ 2, ԁͼѯÇ 1,3 Ւ1 ʹΧ¸ɝ͹ͧҮՕ2 ˈÙʹθƺՕ3 ʹΧ¸CSRS,Փ
)ΚΕ*³±yr·Tϩͪё Fusarium sp. RK97-94 4͹ͺAfïİǇŎűͧN.eՕϳЩŻʼԉṷ̈́Ⱦ
jί?Օ8 ӟêǇ3dQf͹űɐӟêǇy±¹N͹űɐ=gf%ɑ&T³±yr·͹űɐӟêǇSΩƳóŦȮRozµ¦o· B НȾӟêǇ¦¹u¹jͻ/M/f4ՕȢҮҸɺóSºӧR2/Mozµ¦o· B ǉƞ½NёóSՍсŎ4Ѽǡ=gG%ozµ¦o· B ĮʹRcfёóSՍсŎTӴ͹ƣ˗R
2/Maұ;JG%ՍсŎT©±·͹űɐԉǘľNɛĸ=gf;O3dՕ©±·͹ͺ4ҎǨ=gM/f;O4ίƅ=gG%ÜƓՕozµ¦o· B SÑ˹áҚͺͧ͹ͺYSȦԪjѾˊ?G%)ʘ̥OϹˌ*ozµ¦o· B Įʹ?GƧԸ̶NTՕ³±yr·S͹ͺȾ4 5 ĉνȑ¼ʢ?M/f;O4ʣd3RQJG%³±yr·͹űɐTϩͪёR29fÑ˹áҚzµ¹³´x­´¹¹LaeA S
t³µz Lae1 Rceĸȯ=gM/f;Ojѷį?M/f4Օlae1 ΩƳ˗R2/MTozµ¦o· B ̼ŅRcf͹ͺҎǨTҍ`dgQ3JG%;S;O3dՕozµ¦o· B Söͻ͚T Lae1 S¼̮Rǉƞ?
M/f;O4ίƅ=gG%ºʘՕ³±yr·͹űɐӟêǇy±¹ÂSĸȯƔǇĊѰSӟêǇΩƳ˗
R2/MTՕozµ¦o· B Sňˌ4ҍ`dgG%ÜƓSϹˌceՕ³±yr·͹ͺSĸȯª³
jɷǓ?G%
Induction of secondary metabolite production in the lucilactaene producing fungus Fusarium sp. RK97-94
treated with hygromycin B
Sho Kato1, 2, Takayuki Motoyama1,3, Takashi Kamakura2, Hiroyuki Osada1,3 (1Antibiotics Lab, RIKEN, 2Tokyo Univ. of
Sci., 3CSRS, RIKEN)

P-88
rw

·3d²

· A YSƷɺRԅifӮϰӟêǇSɵϱŅѠΛ˴ 1ՕJae-Hyuk JANG2ՕԿ˵ăÑ 1ՕJong Seog AHN2ՕԁͼѯÇ 1 Ւ1 ʹΧ¸CSRSՕ2KRIBBՓ² · A T4kϳЩSȢɋȢɐjԉǘAf̭Ⱦjɫ˰R?M Fusarium sp. FN080326 ceŘԝ=g
GáҚͧN.eՕ®¹yQÓ͸ȾSʗѸ͙ϰԾ˚jʸAf%Fusarium ǳϩͪёSáҚͧO?M΢dgfr
w ·j͹űɐÂԄóRՕͨȴΕQ͸ˬӏjʸAfˀŎűͧRƷɺ=gfOÏɇ=gM/f%͹űɐϸҴѾʣjΚΕR;g]NՕ͹ͺё FN080326 ˗S±|¨Ѿґceѷį?G PKS-NRPS o²ӮϰӟêǇjŶ_͹űɐӟêǇՒfsaՓy±¹jĊѰRѾˊjѦJM5G%ˀΧσNTՕӟêǋΕѾˊRc
e fsa y±¹RŶ]gf͹űɐӟêǇSȧŀSųǓՕͨRÏɇÂԄórw ·3d² · A YSƷɺRԅifӟêǇSųǓj҉^G%
PKS-NRPS o²ӮϰՕ2cW C6 ƣҸĩ̭ȾŎƔǇjEgFg}¹?M/f fsa1Օfsa5 SӟêǇΩƳRceՕ² · A QdWRrw ·S͹ͺ4̵ƿ?G%;SϹˌTՕˀӟêǇy±¹4
Fusarium sp. FN080326 R2/M² · A ͹űɐRԅ¿?M/f;Ojί?M/f%]GՕ;gdΩƳ˗SƧԸ̶Rrw ·j̼ŅAf;ON² · A ͹ͺ4ƓȰAf;O3dՕrw ·4²
· A S͹űɐÂԄóN.f;O4έҍ=gG%y±¹RŶ]gfӟêǇSΑͲ4ƺȊRï½?M/f
fsa5 ӟêǇΩƳ˗R2/MaƷɺ4˧į=gG;OՕy±¹RŶ]gfßSӟêǇSΩƳǕԽjѦJMaՕrw ·3d² · A YSƷɺ̭Ⱦ4ƿigGƷ·˗4ȮdgQ3JG;O3dՕƷɺjɣ0ӮϰӟêǇT fsa y±¹SƸRǉƞ?M/f;O4Ƞ7ίƅ=gG%
Search for genes involved in the conversion from equisetin to fusarisetin A
Naoki Kato1, Jae-Hyuk Jang2, Shunji Takahashi1, Jong Seog Ahn2, Hiroyuki Osada 1(1RIKEN CSRS, 2KRIBB)

 79 —P-89
Aspergillus nidulans SïӯϰҎǨȾЯ®w·ŎӮϰS˶ЫԊӧƾѦՕˠǭăÝՕԿҝΛ˴ Ւϒ̧ƺԍ¸͹ž͸ưՓt´w·ՒTrxՓTɝӯŎ·yҮO?M΢dgՕ̭ȾӧîjˬɐAf CXXC m§ӯөĲª¹
RcJMͨȴà9dgf%Trx TģMS͹ͧRʬӕΕRǉƞ?ՕES˶ЫTΟёՕ˦ͧ2cWŊͧjŶ_y·NĄǉ=gM/f%ӄȌՕζӘTϩͪё Aspergillus nidulans 4ïӯϰ˅å½N Trx ˭S·yҮj}¹AfӟêǇSΑͲ4ҎǨ=gf;Ojʣd3R?G4ՕEgdS͹ʹǋΕ˶ЫTʾHʣd3R=gM/Q
3JG%ïӯϰҎǨȾ Trx ˭·yҮSºKN.f AN6915 TՕ·yҮSЯ®w·ŎRԅifO
Ïɇ=gf PUL ©o·O PPPDE ©o·ՕE?MӯŎӡḙ̌Ⱦjɣ0OÏɇ=gf Trx ©o·3dQ
f©o·ˬӏjʸAf4Օ;Sc0Q©o·ˬӏjɪK·yҮTuRͨȴΕRѷdgf%
ˀΧσNTՕζӘTՕin vitro SǕԽϪjͻ/ՕϷɺ1 AN6915 4·yҮSЯ®w·Ŏ2cW³nϹűSӡḙ̌ȾjɪK;OOՕϷɺ1 AN6915 4®w·Ŏ·yҮSáҚRӳѵQ«¢µ·˭ ATPase N.f Cdc48p (AN7254)OΜÒöͻAf;Ojʣd3R?G%]GՕpq·µn·zѾˊRcJMՕAN6915 SӟêǇΩƳ˗NTՕϳЩħS®w·Ŏ·yҮS¹·4Ӵ͹ƣ˗SE
gO·Qf;Ojѷį?G%â¼SϹˌ3dՕA. nidulans 4ïӯϰ͸ưRȺϓ?ՕAN6915 Sė5jӍ?M®
w·áҚjƷŎ=Cf;ORcJMϳЩħ·yҮSİѾjĸȯ?M/f;O4ʣd3OQJG%
Aspergillus nidulans thioredoxin-like protein functions under hypoxic conditions.
Hiroyuki Abe, Shunsuke Masuo, Naoki Takaya(Faculty of Life and Environmental Sciences, Univ. of Tsukuba)

P-90
Պёm³ CoA űɐӮϰ˸ƿ˗RcfӓԝЬФӯSԿ͹ͺͰӴǊº 1ՕKenneth S. Bruno2Օǩ̗щʣ 1ՕΥÔʰǇ 1Օ»̰ɉ 1Օǵ˙ČǇ 1Օˡ˄мǇ 1ՕScott E. Baker2Օ΀ͼԚÇ 1Ւ1 ͺІΧ¸͹ͧµՕ2 ϟƚny¹prƚχΧσɕՓ ŎΥͣʔSÀ΂ΕQԡѵSƱŅRë/Օot¦QPS˦ͧɐİ3d͸ưYSҡюSǪQ/otͣʔj͹ͺAfəѧ4̔`dgM/f%E;NՕՊё Aspergillus oryzae ϑSϩͪёTͧҮİѾOűɐSЫŃRęgM/f;O3dՕ;SЫŃj̭3?MՕʳRáҚȀǋΕQӟêǇʇƷjԼùAf;ORceՕotͣʔbESŞʔjԿ͹ͺAfəѧԃΑjӑ`M5G%ՊёSöfЬФӯbЬФՒ²z² ²ՓTotn¹
³SŞʔO?MĶͻ4ūЫQ;O3dՕ;gdSԿ͹ͺŎj;g]NRÂȶΕR҉^M5G%
 ЬФӯáҚRTƹʎSӮϰ4ԅ¿Af4ՕES0ISm³ CoA űɐӮϰTՕӓԝЬФӯjm³ CoARƷɺAfŤȺjѿǆAf%ESȧŀTՕЬФӯb²z² ²SűɐOİѾSÁʘRԅ¿Af%ˀΧσNTȡӮϰӟêǇR̨Κ?ՕESΑͲjӟêǇϷɺ1RceƷŎ=Cf;ONЬФӯS͹ͺȾŵ¼j҉^G% ]BՊёSȡӮϰӟêǇSɵϱjѦJG%Ӯ̋ S. cerevisiae b A. nidulans ϑßSΟёNųǓ=gM/fȡӮϰRǣ?MՊё|¨SģЙ҆ͺͧjΜųȾ˧ϱ?GϹˌՕȡӮϰRͨȴΕQ©o·SөĲjʣέRaKӟêǇ4 6 Ĉέҍ=gG%˹R;gdSŰΩƳ˗jöѱ?ՕёóħЬФӯӵϑjғZG%ESϹˌՕȡ£ªµzSħS 1 ĈS˸ƿ˗NՕёóħЬФӯӵ4ƺ57ŵ¼?G%ºʘՕßS 5 ĈT˸ƿ?MaՕёóħЬФӯӵ4ŵ¼?Q3JG%ͲƞՕЬФӯ͹ͺӵ4ŵ¼?Gȡ˸ƿ˗S|¨ΑͲɆƬjѾˊ?ՕЬФӯűɐSȪӎOQJM/fáҚŤȺjÏͅ?MՕEgjϷɺ1RceȠŎAf;ONՕʳQfŵ¼jΚɫ?M/f%
Increased Production of Free Fatty Acid by the Acyl-CoA Synthetase Disruptant of Aspergillus oryzae
Koichi Tamano1, Kenneth S. Bruno2, Hideaki Koike1, Tomoko Ishii1, Ai Miura1, Noriko Yamane1, Myco Umemura1,
Scott E. Baker2, Masayuki Machida1 (1AIST, 2PNNL) 80 —P-91
o/aIΎёS Ehs1 SympՕyp·R29f
ѫͲƣS̎ҺO˹Àá¹{·¹Rcf±·y²¹¨Ѿˊ˄ӴɎǀՕȖ͓ɦȄՕɐǿɂՕэ̼ҧÇ, ʗÔſр, ƺԀ͒, ˞ͼъ, ӽćԿȹ (ˈʹƺԍʹȀ¸Ⱥ͹θ)o/aIΎёToRɊˑ?o/aIΎjț5ұ;A˦ͧΎŞϩͪёN.f%ˀёSİ͹ǇTǛÄѫԦ
RàΠAfOΑц?ՕɊˑRȷԭQàΠƏO/0ˬӏjȢɐAf%;SԕՕΑцϗìԁʪbàΠƏȢɐʪS
àΠƏħӧN Ca2+͕ȑ4¼ʢAf;O4΢dgM2eՕ;g]NSΧσN Ca2+«³ԉǘľS̼ŅRcJMՕàΠƏȢɐͯ4͕ȑýǉΕRï½Af;O4İ3JM/f%ȡΧσǖNTՕΎŞȾԅӐӟêǇO?MՕİѭӮ̋R29f˶ˣĹ͔öŊƣSìǲ̭ȾŎ Ca2+«³S£ªµzN.fOɷǓ=gf Ehs1 S˶ЫѾˊjѦJM2eՕymp˗jöѱ?GO;hƚͺӴ͹˗ P2 O̎Һ?MàΠƏȢɐͯՕ˖ԸёϩɐԁR2/MʸɈQȂ4ѷdgQ3JG%?3?Օo/aIΎё Br48 ˗ͽˆS Ehs1 yp·˗NTӴ͹˗O̎Һ?MàΠƏȢɐͯՕ˖ԸёϩɐԁՕЩǇȢɐЫ4́Ǫ?M/fO/0Ƭź4Q=gG (Nakayashiki, et al.,2008) %E;NȡΧσǖN P2 ˗ͽˆS GFP ȿȉΑͲ˗ MK2-2 jͻ/ՕEhs1 yp·˗jöѱ?GO;hՕàΠƏȢɐͯՕ˖ԸёϩɐԁSï½4ѷdgՕESßRa}·µ¹³O̎Һ?M/7K3ȢҮRȂ·
4͹@G%â¼S;O3dՕˀΧσNTymp˗Oyp·˗NȢҮRȂ4ѷdgGŞƔjѾʣ
Af;OjΚΕO?ՕѾˊjѦJG%;g]NSϹˌceՕymp˗Nôd3S˶ЫΜѰ4ұ5GūЫȾ4Л1dgGG`ՕӴ͹˗ P2 O Ehs1 ympšWyp·˗RK/M˹Àá¹{·¹jͻ/G±·y²¹¨ѾˊjѦ/ՕΜѰƔǇSɵϱjѦJG%
Transcriptome analysis and comparison of phenotype with disruptant and knockdown mutant of Ehs1 in
Pyricularia oryzae
Keina Murano, Takumi Hirosawa, Megumi Narukawa, Takayuki Arazoe, Jun Ohgane, Shigeru Kuwata, Takashi
Kamakura (Dept. of Applied Biological Sci, Tokyo Univ. of Science)

P-92 (O-18)
Ŏűͧm´ojͻ/G©±·͹űɐԉǘľɵϱˀǵԿȍ 1,2ՕͼÂԑǇ 2ՕԁͼѯÇ 1,2Ւ1 ʹΧ¸ɝ͹ͧҮՕ2 ʹΧ¸CSRSՓ
【目的】イネいもち病菌の二次代謝産物メラニンは病原性に必須であるが生育には必要とされないため，生合成系の酵素は環境負荷が低い農薬の標的として注目されてきた。メラニン生合成系の 2 種類の標的酵素（3HNR，Sdh1）に対する農薬（MBI-R，MBI-D）が開発されてきたが，既存の農薬は耐性菌などの問題を抱えており，新たな制御薬剤の開発が求められている。我々は，天然化合物バンク NPDepo を設立し，標的タンパク質に対する結合化合物探索を超ハイスループットで行うことが可能な化合物アレイを開発してきた。
今回，化合物アレイを用いた NPDepo 化合物からのメラニン生合成阻害剤探索について報告する。
【方法と結果】メラニン生合成系の標的酵素として，非還元型ポリケタイド合成酵素（NR-PKS）Alb1，ヒド
ロキシナフタレン還元酵素 3HNR，シタロン脱水酵素 Sdh1 を選択した。Sdh1 については，野生型酵素 Sdh1-WTと農薬耐性型酵素 Sdh1-V75M を用いた。それぞれの標的酵素を大腸菌で発現・精製し，化合物アレイスクリー
ニングを行った。NPDepo の約 3 万化合物の中から，Alb1，3HNR，Sdh1-WT，Sdh1-V75M に対してそれぞれ，
21 個，21 個，4 個，8 個のヒット化合物を得た。3HNR のヒット化合物の阻害活性を解析したところ，1 化合物（リファマイシン誘導体）が阻害活性を示した（IC50=25 µM）。従来のスクリーニング法と化合物アレイによるスクリーニング法との違いについて報告する。
本研究の一部は，農林水産業・食品産業科学技術研究推進事業による支援を受けた。
Chemical array screening of melanin biosynthesis inhibitors
Takayuki Motoyama1,2, Yoko Tanaka2, Hiroyuki Osada1,2(1Antibiotics Lab, RIKEN, 2CSRS, RIKEN) 81 —P-93
MAP w¹ Pmk1 T H3K4 ·©³ƨҸλӮϰ MoSET1 S¼̮N˶ЫAf
Nguyen Hieu Hanh, Kieu Thi Minh Pham, ̗ͼďº, ÂǱʐƢ Ւβɓƺ¸ԍӀՓȡΧσǖNTՕoθ˦ͧ/aIΎёS H3K4 ©³Ŏjɣ0 MoSET1 SΩƳ˗Ւ"moset1Փjöɐ?ՕE
SȾ˚à9RK/MʨȌSˀǋéNƬź?G%"moset1 NTՕàΠƏȢɐͯ4ƺȊRï½?ՕǛÄ˦ͧR2
9fΎŞȾjǎģR̵ƿ?M/G%;gdSѼǡb/7K3SӟêǇSΑͲ¹·SѾˊ3dՕ"moset1
O MAP w¹N.f Pmk1 SΩƳ˗SѫͲƣRTԲí͚4.f;O4ίƅ=gG%E;NÜƓՕMoSET1
O Pmk1 SӟêΕ¼îȾRK/M˧҂?G%ȡΧσǖNùͻ?M/f Br48 ˗S Pmk1 SΩƳ˗("pmk1)jöɐ?ՕChIP-qPCR ѾˊjѦJGɕՕӴ͹˗NTàΠƏȢɐʪR H3K4me2 ´¡³S¼ʢ4ҍ`dgfӟêǇȒîNaՕ"pmk1 NTES´¡³¼ʢ4ҍ`dgQ3JG%]GՕRNA-seq ѾˊϑNųǓ=gG Mo-SET1
Rýǉ?MΑͲ¼ʢAfƹ7SӟêǇ4"pmk1 NTŤȺȾjί=Q7QJM/G%ºʘՕ"moset1 R2/M
a Pmk1 ӟêǇSΑͲ´¡³TʸɈQȦԪjŧ9M/Q3JG%â¼S;O3d Pmk1 T MoSET1 ceӟêΕ¼îRîГ?ՕΛɶ.f/TԄɶΕR MoSET1 S̭Ⱦjғϙ?Օ/aIΎёR29fàΠƏȢɐϑRȷѵ
QӟêǇSΑͲjĸȯ?M/f;O4Л1dgG%

The MAP kinase, Pmk1 is epistatic to MoSET1, H3K4 methyltransferase for infection-related morphogenesis in
Magnaporthe oryzae
Nguyen Hieu Hanh, Kieu Thi Minh Pham, Ken-ichi Ikeda, Hitoshi Nakayashiki(Grad. Sch. Agr., Kobe Univ.)

P-94 (O-19)
p²Բ͙ΌΎёR29fįцӮ̋´ȺϓĸȯƔǇ WHI2 S£ªµz CoWHI2TǛÄԈȯȺϓSҎǨO͉̭ͧǜ͹ȾSĸȯRԅ¿AfŞͼ Ҭ, ÆĄȔÇ (ÙȐƺԍ¸͹͸)ʨȌȑSˀéRM,p²Բ͙ΌΎёS CoRas2 TɊˑƏǑSȢɐӖνRo§yQǯƞjίA;OjƬ
ź?G%įцӮ̋S Whisky2(Whi2)T Ras SϳЩħǯƞSĸȯbsl¹j}¹Af Psr1 OϹűAf;ORceҸĩƔǇ Msn2 jЯ²·ӯŎ?, STRE(Stress response element)jʸAf´ҎǨӟêǇSΑͲjĸȯAf;O4Ƭź=gM/f%E;N,Ras SʪτԄΕQĸȯOɊˑƏǑSȢɋȢɐSԅāRK/M
ғZfG`R,ɑ&Tp²Բ͙ΌΎёR29f WHI2 S£ªµz CoWHI2 RΠΚ?,˶ЫѾˊjѦJG%]
B,CoWHI2 4ΎŞȾbɊˑƏǑSȢɋȢɐRԅ¿AfS3,cowhi2 ˗jöį?,˧҂?G%ESϹˌ,cowhi2
˗Sw­p²RǣAfΎŞȾTӴ͹˗O̎Һ?,ï½?G% ]G,cowhi2 ˗SÿĢёϩTӴ͹˗O̎Һ?,́ͧǜ͹Ⱦ˭Sϳ/Ȣɋjί?G%кż̹/;OR,cowhi2 ˗TӴ͹˗O̎Һ?,ǛÄ˦ͧSuµ¹ȢɐjԱјRҎǨ?G%E;N,cowhi2 ˗Tuµ¹ȢɐRԅifuµ¹űɐӮϰӟêǇSΑͲjҎǨAfS3,
cowhi2 ˗ɶοїSuµ¹űɐӮϰӟêǇSΑͲӵj qRT-PCR jͻ/,ϸʪΕRͅǓ?G%ESϹˌ,
cowhi2 ˗ɶοїNTӴ͹˗ɶοїO̎Һ?,ʟʼRµo ATGSL4,ATGSL8 S£ªµzSΑͲӵ4Ʊ
Ņ?G%;S;O3d,CoWHI2 Rcfuµ¹ȢɐSҎǨT;gdSuµ¹űɐӮϰӟêǇRұƔAfūЫȾ4ίƅ=gG%˹Rcowhi2 ˗T́ͧǜ͹˭ÿĢёϩjȢɐ?G;O3d,́ͧǜ͹ёRǣ?ΑͲ4ƱŅ
AfµoS PDF1.2 Sw­p²R29f£ªµz DEFENSIN19 SΑͲӵj qRT-PCR jͻ/,˧҂?
G%ESϹˌ,cowhi2 ˗ɶοїS DEFENSIN19 SΑͲӵTӴ͹˗ɶοїO̎Һ?,ԱјRƱŅ?G%â¼3d,CoWHI2 TǛÄԈȯȺϓSҎǨO͉̭ͧǜ͹ȾSĸȯRԅ¿Af;O4ίƅ=gG%
CoWHI2, the homolog of stress response regulator WHI2 of Saccharomyces cerevisiae, is involved in induction ofhost defense response and regulation of hemibiotrophic infection in Colletotrichum orbiculare.
Ken Harata Yasuyuki Kubo (Life and Environmental Sciences, Kyoto Prefectual Univ.) 82 —P-95
p²Բ͙ΌΎё GAP Ѳűó CoBub2/CoBfa1 T GTPase CoTem1 jÝ?M G1/S ʼӑѦĸȯ2cW˦ͧɊˑRǜ¿Af̹ͼŭЕՕơũ ˿ՕÆĄȔÇՒÙӨȐƺԍ¸͹͸Փ
p²Բ͙ΌΎёTɊˑӖνR2/MՕŘϳЩSЩǇ3dΑцϗՕàΠƏՕÿĢёϩSȢɐO/JGłΕQȢɋİŎj˘İѭOųғŎ?MѦ0%ɑ&TįцӮ̋R2/MMʼ϶Î˶ˬjĸȯAfBUB2S£ªµz
CoBUB2jųǓ?ՕˀӟêǇ4G1/SʼSӑѦjĸȯ?ՕÿĢƏǑSȢɋİŎ2cWΎŞȾRȷԭN.f;OjºʨȌȑSˀéRMƬź?G%ÜƓՕCoBub2Sz³u{¹SѾˊjѦJG%]BՕįцӮ̋R2/
MBub2OGTPasḙȾŎ·yҮՒGAPՓѲűójȢɐAfBFA1S£ªµzCoBFA1SΩƳ˗jöį?ՕȢ
ҮS҈þjѦJG%ESϹˌcobfa1Tcobub2Oų˭S˸ɽȢҮjί?ՕG1/SʼSλѦʪʼSĂӑՕÿĢƏǑSȢɋ·ȉOǛÄ˦ͧYSΎŞȾSï½4ҍ`dgG%=dRՕįцӮ̋R2/MBub2/Bfa1Rce¾̭
ŎSĸȯjŧ9fïİǇӵGTPase Tem1RΠΚ?Օcobub22cWcobfa1Rȿȉ¾̭ȾƣCoTEM1jǨĢA
f;ORceՕΩƳ˗S˸ɽȢҮ4ΜѰ=gf3˧҂?G%ESϹˌՕȿȉ¾̭ȾƣCoTEM1ǨĢ˗NTΩƳ˗Nҍ`dgfϳЩŻʼ2cWȢɋȢɐՕΎŞȾS˸ɽȢҮ4ΜѰ=gՕӴ͹˗Oų˭SѫͲȢjί?G%â¼ceՕCoBub2TCoBfa1OŖų?MGTPase CoTem1jÝ?GG1/SʼSӑѦĸȯ2cWÿĢƏǑȢɐՕǛÄ
YSΎŞȾRԅ¿Af;O4ί=gG%
Colletotrichum orbiculare CoBub2/CoBfa1 GAP complex regulates G1/S progression and plant infection via
GTPase CoTem1
Fumi Fukada, Ayumu Sakaguchi, Yasuyuki Kubo
(Life and Environmental Sciences, Kyoto Prefectural Univ.)

P-96
p²Բ͙ΌΎёR29f MOR z³êӘϸҴTǛÄ˦͎ͧį̶ÂSy·ª¦¹ҍқjÝ?GàΠƏȢɐRԅ¿AfǩͰϯáՕơũ ˿ՕÆĄȔÇՒÙӨȐƺԍ¸͹͸Փ ļƓՕɑ&T˦ͧΎŞϩͪёp²Բ͙ΌΎёR2/M˦ͧѫԦSͧʹΕz³ŧǚjÝ?GàΠƏȢɐ
RϳЩ˪ȾĸȯƔǇ CoKel2 4ԅ¿AfºʘNՕ˦ͧͨ·Εz³ŧǚjÝ?GàΠƏȢɐRTįцӮ̋S
ϳЩ˪ȾɐԁbİԝQPjĸȯAf MOR [morphogenesis-related NDR (nuclear Dbf2-related) kinase network]SˬɐƔǇ Pag1 OΜųȾjaK CoPag1 4ԅ¿Af;OjƬź?G%]GՕCoPag1 T MOR ˬɐƔǇ Ndr w¹
 CoCbk1 S̭ȾĸȯRԅ¿?ՕMOR T˦ͧͨ·Εz³ŧǚϸҴRԅ¿AfūЫȾjί?G%ÜƓՕ
CoPag1 S˦ͧѫԦͧҮҍқjÝ?GàΠƏȢɐYSԅ¿j҈þAfG`RՕw­p²͎į̶ǉƞ½SÛȀƨ
Ү¼R29fàΠƏȢɋjѼǡ?G%ESϹˌՕcokel2Δ T͌ё̒ƧԸʪO̎Һ?Mw­p²͎į̶ǉƞ½N
˽ȉàΠƏȢɐ4ƓȰ?GSRǣ?MՕcopag1Δcokel2Δ S˽ȉàΠƏȢɐTƓȰ?Q3JG%;S;O3dՕCoPag1 TǛÄ˦͎ͧį̶ÂSͧҮҍқjÝ?GàΠƏȢɐRԅ¿Af;O4ίƅ=gG%˹RՕ˦ͧͨ·Εz³ŧǚϸҴRceҍқ=gf˦ͧz³jųǓAfG`RՕy·ª¦¹SºKN.f 1,
16-hexadecanediol 2cWw­p²͎į̶Â3dųǓ?G Octadecanal ǉƞ½SÛȀƨҮ¼R29fàΠƏȢɋ
jѼǡ?G%ESϹˌՕcokel2Δ T˽ȉàΠƏȢɐ4ԱјRƓȰ?GSRǣ?MՕcopag1Δcokel2Δ S˽ȉàΠƏȢɐTƓȰ?Q3JG%â¼SϹˌ3dՕCoPag1 4ԅ¿Af˦ͧͨ·Εz³ŧǚϸҴTy·ª¦¹SҍқjÝ?GàΠƏȢɐRԅ¿AfūЫȾ4ίƅ=gG%
Colletotrichum orbiculare MOR signaling pathway is involved in appressorium development triggered by cutinmonomers in the host plant exudate
Sayo Kodama, Ayumu Sakaguchi, Yasuyuki Kubo
(Life and Environmental Sciences, Kyoto Prefectural Univ.) 83 —P-97įцӮ̋ ·²·zѾԝƔǇ   Sp²Բ͙ΌΎё£ªµz   TàΠƏÿĢёϩȢɐ̆ԓSmy·Ŋɋjĸȯ?ΎŞȾRԅ¿Afǿϊ ʠ, ̹ͼŭЕ, ơũ ˿, ÆĄȔÇ ՒÙȐƺԍ¸͹͸Փ;g]Np²Բ͙ΌΎёR2/M, įцӮ̋S RTS1 S£ªµz CoRTS1 SΩƳ˗jȮM/f%įцӮ̋R
2/M Rts1 TϳЩҮİѭǎÎʪRİѭ͊Rǯƞ?, ϳЩҮİѭԅӐİǇSҳƭN.f ·²·zjѾԝAf˶ЫjɪK%ºʘ, p²Բ͙ΌΎё corts1 ΩƳ˗TϳЩҮİѭ4ʾǎÎSͪɋSЩǇ4ǉƞ?àΠƏȢ
ɐͯ4ԱјŔǪ?G%CoRTS1 SàΠƏȢɐ̆ԓR29f˶ЫjғZfG`, įцӮ̋R2/M Rts1 Sǯƞ̙ǓӧîN.f N ʿϊm§ӯ 100 ̄ƨj}¹AfƯƨj˸ƿ=CG corts1!100 jöį?G%corts1!100
T M ʼSӒȗbmy·ŊɋS·ȉjί?, Αцϗ4ìԁ?̧ɘJG·ȉàΠƏjȢɐ?MΎŞȾ4ï½?
G%įцӮ̋NT˪ȾɐԁʪS ·ŊɋR˸ɽ4͹@Gԕ, M ʼ4Ӓȗ?˪Ⱦɐԁ4Ё7;O4΢dgM
2e, ;SϹˌ3d CoRTS1 TįцӮ̋O·Qe, ˪ȾɐԁʪRa ·ŊɋRԅ¿AfūЫȾ4ί=gG%;SūЫȾj˧҇AfG` ·Ʒ·˗!cocdc12 jöį?, ѫͲƣjғZGϹˌ corts1!100 ų˭RΑц
ϗ4ìԁ?GȢɋjί?, ãҐjʆɪAfϹˌ4ȮdgG%Ͳƞ,·ŊɋS˸ɽRǣȺAfG`ϳЩŻʼjӒȗ=Cf SWE1 S£ªµz CoSWE1 OȢɋȢɐSԅāRK/MѾˊjӑ`M/f%
CoRTS1, the homolog of Saccharomyces cerevisiae RTS1, a septin ring disassembling factor, is involved inpathogenicity by regulating actin dynamics during appressorium and invasive hyphae formation in
Colletotrichum orbiculare.
Kou Kawabata, Fumi Fukada, Ayumu Sakaguchi, Yasuyuki Kubo
(Graduate School of Life and Environmental Sciences, Kyoto Prefectural Univ.)

P-98
͗с3WΎёR29f 26S µm¹¨® RPN10 £ªµzSѾˊðͼŕË 1Օ̣̬Ȝò 2ՕͼÂŒǦ 1Ւ1 Ùƺԍ¸ӀՕ 2 ͍ҩΞƺ¸͸ưθǋՓ®w·¸µm¹¨ϪՒUPSՓT®w·ӾRcJM˰қ=gG·yҮjӞɟΕRİѾAfϳЩħзȃİѾϪN.eՕΟ˘͹ͧRȎ7Ąǉ=gM/f%?3?ϩͪёԲR2/MT UPS RԅAf΢ѷ
TʾHǪQ7ՕOei9 UPS R2/MƨҮİѾjɣ0·yҮİѾӮϰѲűóµm¹¨SȧŀRK/MT[OkPʣd3R=gM/Q/%įцӮ̋µm¹¨S® RPN10 TՕ®w·ŧǚóO?M˰Ε·yҮjҍқAfO
OaRՕµm¹¨зҶSǍǓŎRaǜ¿?M/fO=gf%ˀΧσNTÀ΂ΕRӳѵQƹͩȾ˦ͧΎŞёN.f͗с3WΎёR2/MՕįцӮ̋ RPN10 S£ªµz BcRPN10 SӟêǇΩƳ˗jöį?ՕES˶ЫѾˊjѦJG%BcRPN10 ΩƳ˗TӴ͹ƣ˗O̎Z}µ¹͹Х4bbӒ7Օİ͹ǇȢɐʎ4ј?7ï½?
G%ï̈́˅å½NTՕӴ͹ƣ˗4ΗkRё˘jȢɐAfSRǣ?ՕBcRPN10 ΩƳ˗Tё˘jģ7Ȣɐ?Q3J
G%]GՕo·|·¦©Rǣ?MёŨͤjͻ/Gɶο҉ԽjѦJGO;hՕBcRPN10 ΩƳ˗TǛÄ¼NɊˑ
ƏǑN.fàΠƏ2cWɊˑȒjȢɐAf;O4N5G4ՕΎʓjȢɐAf;O4N5Q3JG%ESºʘNՕBcRPN10 ΩƳ˗TʸĔɶοR2/MTΎʓjȢɐAf;O4N5G%;gdSϹˌ3dՕ͗с3WΎё
R2/Mµm¹¨jÝ?GƨҮİѾ4ŰοȢɋȢɐՕǛÄÿĢRӳѵQȧŀjˌG?M/fūЫȾ4ίƅ=gG%
Characterization of 26S proteasome subunit gene RPN10 of Botrytis cinerea.
Takuya Sumita1, Kosuke Izumitsu2, Chihiro Tanaka1(1Grad. School of Agriculture, Kyoto Univ., 2Sch. Of Environmental Science, Univ. of Shiga Pref.) 84 —P-99
pªµ}<]їˎΎёS CHK1 MAPK ϸҴSɷǓ¼̮ƔǇS˶ЫѾˊŏįԙ͹ 1Օ̣̬Ȝò 2ՕðͼŕË 1ՕͼÂŒǦ 1 Ւ1 Ùƺ¸ԍ¸ӀՕ2 ͍ҩΞƺ¸͸ưθǋՓ
pªµ}<]їˎΎёTpªµ}SʶӳѵΎǘёSVOKN.f%ɑ&TˀёɊˑR29fĳʼ
̆ԓN.fàΠƏȢɐRȷԭQ CHK1 MAP w¹ϸҴR̨Κ?, ESԅӐƔǇjųǓ¸˶ЫѾˊAf;O
RceՕàΠƏȢɐʪR29fz³êӘSģǚѾʣjΚɫ?M/f%ɑ&TʨȌȑSˀéR2/M, ˀϸҴSɷǓ¼̮ƔǇN.f 2 οԲS PAK ˭w¹RK/M, CLA4 4àΠƏȢɐbȢɋȢɐģоRӳѵQ
ȧŀjɪI, STE20 TʸȾ͹̅S^RӧİΕRԅ¿Af;OjƬź?G%ÜƓɑ&T PAK ˭w¹SɷǓ¼̮ƔǇN.fïİǇӵ G ·yҮ CDC42 QdWR RAC1 j}¹AfӟêǇSΩƳ˗jʗGRȢɋȢɐ҉ԽRü҉?G%;gdģMSΩƳ˗SȢɋȢɐ·ȉT Δchk1 ceҹȑN.e, Ű 2 οԲSƔǇ4ºǓSӳѲ?G˶ЫjɪKūЫȾ4ίƅ=gG%Δrac1 TàΠƏȢɐЫbʸȾ͹̅ЫSƋƿQP, Δcla4 O[\ų˭
N.f4, ceӳȑQ·ȉjί?G%]GÁΩƳ˗TёϩɐԁʪSд͒bÑŠİˍQP, Δchk1 RTQ/ͨʸSȢҮjĥʸ?M/G%ºʘ, Δcdc42 TàΠƏȢɐʎbİ͹ǇȢɐʎSï½QP, Δste20 QdWR Δcla4 SÂԄΕQȢҮjί?G%â¼SϹˌ3d, RAC1 T CLA4 jÝ?MёϩɐԁQdWRȢɋȢɐjĸȯAf4,
CHK1 ϸҴce_?h ·Ŋɋbmy·ĨˬɐO/JGϳЩİѭ¸ϳЩ˪ȾSĸȯƔǇO?MöͻAfūЫȾ4ίƅ=gG%]G, CDC42 T STE20 H9NQ7, CLA4 bESßSƔǇS¼̮ƔǇO?Möͻ?M/fūЫȾ4ίƅ=gG%Ͳƞ;gd¼̮ƔǇԄSΜÒöͻRԅ¿AfūЫȾ4ίƅ=gfm¹·yҮ BEM1 SӟêǇΩƳ˗öįj҉^M2e, ˀΑѫNT BEM1 S˶ЫRK/MaøCM˧҂AfÏǓN
.f%Characterization of putative upstream factors of CHK1 MAPK pathway 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-100ԥΎŞȾ Alternaria alternata ё˗YSǛÄͨ·Ε AAL ̍ϰ͹űɐӟêǇy±¹SǨĢԿǭſǕ 1ՕүʽԣĦ 2Օ˒˦ǫȹ 3ՕġͰƨºʺ 1 Ւ1 ՄŦӐƺ¸2 ՄŦƺӀ¸3 Ŵƺԍ͹ӀՓ ¦m³¹²mыˎΎё (Alternaria alternata tomato pathotypeՕыˎΎё) TǛÄͨ·Ε AAL ̍ϰj͹ͺAf;ONՕͨǓS¦ƀοRΎ̑jț5ұ;A%ˀ̍ϰS͹űɐTՕǪQ7Oa 13 ӟêǇ3dQf
AAL ̍ϰ͹űɐӟêǇ (ALT) y±¹4ԅ¿AfO=gM/f%ALT y±¹TыˎΎёS^4ĄʸA
f 1 Mb S CD ˑсóRϬ 100 kb RiGJMȒÉ?M/f%ȡΧσǖNT CD ˑсóS̒ȋλŊRceՕԥΎŞȾё4ΎŞȾjͭȮAf;OjƬź?M/f%ºʘNՕˀy±¹ӟêǇS^NՕёR̍ϰ͹ͺЫjҭ¿N5f3Tʣd3OQJM/Q/%ˀΧσNTՕ4 ʕͤRİŀ?G ALT y±¹ӟêǇjՕAAL ̍ϰj͹ͺ?Q/ԥΎŞȾ A. alternata ё˗RǨĢ?G%ESϹˌՕ13 S ALT ӟêǇAZM4ǨĢ=gGūЫȾS.fё˗4ȮdgG%ǨĢё˗T AAL ̍ϰ͹ͺ2cWΎŞȾ4έҍ=gG%
Introduction of entire ALT cluster genes to nonpathogenic Alternaria alternata
Kazumi Takao1, Yasunori Akagi2, Takashi Tsuge3, Motoichiro Kodama1(1UGSAS, 2Fac. Agric., Tottori Univ., 3Grad. Sch. Bioagric. Sci., Nagoya Univ.) 85 —P-101
¦m³¹²mыˎΎёR29f
1

1

2±§űɐӮϰӟêǇS˶ЫѾˊ

3 1үʽԣĦ ՕΥŞ Ø Օ˒˦ǫȹ ՕġͰƨºʺ ( ՄŦƺӀՕ2 Ŵƺԍ͹ӀՕ3 ՄŦӐƺ)˦ͧΎŞϩͪё¦m³¹²mыˎΎё (ыˎΎё) Rce͹ͺ=gf AAL ̍ϰTՕsphinganine
analog mycotoxins N.eՕǛÄ¦S ±§űɐjԉǘAf;ONϳЩ́jҎұAfOЛ1dgM/f%
AAL ̍ϰ͹űɐӟêǇy±¹¼RTՕ ±§űɐӮϰӟêǇ (Cer) £ªµzՒAAL ̍ϰɡɝȾӟê
Ǉ Asc1 £ªµzՓN.f ALT7 (AaLAG3) 4ǉƞAf4ՕˀӟêǇΩƳ˗NTՕAAL ̍ϰ͹ͺЫ2cW AAL̍ϰНȾRƷŎTҍ`dgQ3JG%ыˎΎёS±|¨ѾˊRceՕˀёT AaLAG3 âƸR 2 KS
Cer £ªµz (AaLAG1 2cW AaLAG2) jʸ?M/f;O4ί=gG%;gdӟêǇSΩƳǕԽjѦJGϹˌՕAaLAG1 ΩƳ˗SɐԁTՕPDA 2cW V8 ƧƠ¼Nј?7ӒȗAf;O4ʣd3OQJG%]GՕAaLAG2
ΩƳ˗NT V8 ƧƠNiB3RɐԁӒȗ4ҍ`dgG4ՕAaLAG3 ΩƳ˗NTѻ˗OȂ·T^dgQ3JG%ºʘՕAaLAG2/AaLAG3 ³ΩƳ˗R2/MTՕј?/ɐԁӒȗO AAL ̍ϰ͹ͺSƿ̭4ҍ`dgG՗
Functional analysis of the ceramide synthase genes in the tomato pathotype of Alternaria alternata
Yasunori Akagi1, Atsushi Ishihara1, Takashi Tsuge2, Motoichiro Kodama3(1Fac. Agric, 3UGSA, Tottori Univ., 2Grad. Sch. Bioagric. Sci. Nagoya Univ.)P-102˦ͧΎŞŜё Phytophtora infestans SàΠƏȢɐԉǘͧҮSɵϱǿˀΟËՕ;ʒȘ˹ՕҝĆ̠Օ͙ҝԬºՕǿũĽůՒԇȐƺԍ¸͹͸θՓPhytophthora infestans Tθ˦ͧRɊˑ?΋Ύjț5ұ;A˦ͧΎŞŜёN.f%P. infestans SӓҰǇƐT 15â¼S͸ưNTΛɶΑц?ёϩjìԁAf4 15â½NTӓҰǇjʉįAfĕŵR.f%ʉį=gG
ӓҰǇTҰŎΕR˦ͧĐRӓ̪ȫՕՕàΠƏYOİŎ?˦ͧRɊˑAf%;Sï̈́RȺϓ?GӓҰǇƐİŎ4΋ΎћȗSÄѵϸҴN.faSSՕyµ§΂RǳAf Phytophthora SӓҰǇƐİŎ˶ˬTʾѾ
ʣQӧİ4ƹ/%E;NˀΧσNTՕP. infestans ӓҰǇƐŰİŎ̆ԓjͨ·ΕRԉǘAfͧҮjʉЉё4ͺ͹AfÑ˹áҚͺͧjǣҠO?My²¹·z?ՕųǓ?GͧҮj¹³O?MӓҰǇƐİŎ˶ˬjİǇ´¡³NѾʣAf;OjΚΕO?G%]B§·ӯjŘº͙ϰ͈O?GƧƠjͻ/MʉЉёjӞɟΕRŘԝ?G%ʉЉёSƧԸ̶RϑӵSm·jŅ1GaSj·³O?M P. infestans ӓҰǇƐR̼Ņ?Օ10RԤГ?M 18 ʪԄȫSȢɋjԱȲӿ
½NѼǡ?G%Ϭ 800 ˗Sɢį·³RK/Mɵϱ?GϹˌՕŰİŎ̆ԓjԉǘAf̭ȾjʸA·³
jŦȮ?ՕESÂNaàΠƏȢɐjԉǘ?Gՙ·³RΠΚ?MѾˊjӑ`G%ŦȮ?G·³NĮʹ
?GӓҰǇƐTʾĮʹSӓҰǇƐO̎Һ?M¦SїYSɊˑЫ4ј?7ï½?G4Օ18NSёϩìԁ
2cWӓҰǇƐȢɐRTȦԪ4Ѽǡ=gQ3JG%àΠƏȢɐԉǘͧҮj͹ͺAfՙ˗S 16S ribosomal RNAϪϽѾˊjѦJGO;hՕĥR Streptomyces chartreusis SӄЌοN.JG%ͲƞՕàΠƏȢɐԉṷ̈́ȾSce
Կ3JG no. 287 ˗ͽˆSàΠƏȢɐԉǘͧҮjο&Syµ¦z±n¹RceϦѱ?M/f%
Screening for substances inhibiting appressorium formation of plant pathogenic oomycete Phytophthora
infestans
Masaya Kawamoto, Kenji Kai, Shuji Tani, Jun-ichi Sumitani, Takashi Kawaguchi(Grad. Sch. Life & Env. Sci., Osaka Pref. Univ.) 86 —P-103ƹͩȾ͙ΌΎё (Colletotrichum fioriniae) SɊˑ±o§·zƔǇSɵϱƺԿ͒ÇÝՕ͖ǭъЕ, Ѵ˄ՋӲ̖ Ւ͹ͧΧՓ˦ͧRT, ϩͪёRͨȴΕQϳЩƲˬɐƹϧ (chitin, β-1,3-glucan) QPSİǇ¹·j·ͧ (PAMPs)
O?Mҍқ?ʈʁAfĠ΋˶ˬ (PTI) 4ĒiJM/f%ºʘ, ΎŞёTǛÄS PTI jӠ9M˦ͧħRÿĢ?
ɊˑAf%;g]NSoΎŞȾϩͪёՒǇƐёԲ: o/aIΎё, o~¦їˎΎё, ɣǇёԲ: oϭˎΎёՓSɊˑ˶ˬRԅAfΧσ3d, ;gdSёNT˦ͧɐİ4±o§·zՒŽW̒ՓƔǇOQJMöͻ?, ˦ͧROJMԞİѾȾS α-1,3-glucan jёóѫǴRњς?зҶjĄҜAfOOaR, ϳЩƲ PAMPs
jѶ/ԗA;ONǛÄ PTI jƓӠAf;O4ʣd3RQJG%â¼S;O3d, ΎŞȾϩͪёNTǛÄͽˆS±o§·zƔǇ4ɊˑɐχRӳѵN.fOɷͅ=gf%
Ͳƞ, ɑ&Tс&Q˦ͧՒªµo¬, ²·~, p©QPՓjǛÄOAfƹͩȾ͙ΌΎё (Colletotrichum

fioriniae) jͻ/M, ˀёR±o§·zƔǇO?MöͻAfǛÄ˦ͧͽˆƔǇjʣd3RAfG`R,
α-1,3-glucan SњςbɊˑƏǑȢɐQPjɫ˰Rɵϱjӑ`M/f%ˀΑѫNTȮdgGɐˌRK/MƬźAf%

Investigation of priming factor(s) for Colletotrichum fioriniae infection from host plants
Junnosuke Otaka, Shigemi Seo, Marie Nishimura(NIAS)

P-104 (O-20)¦o}po³ɊˑRcfϩͪёϳЩƲSˬӏƷŎʻʷИǇՕӷʽąȜՕύŞϴ ՒǗƥƺ¸Գͺ˩¸͸ưՕǷǵƺ¸˦ͧΧՓϩͪё Cryphonectria parasiticaՒʝ Endothia parasiticaՓTĭÌ̭ȾjίAӯȾµm¹jԿͺ͹?Օi4ƚNaŪ73dΧσǣҠO=gM5GϩͪёN.f4Օy²QPSˌ˴Rǣ?MЪˎΎjț5ұ;A˦ͧΎŞёNa.f%100 ȌõeļRʜˀ3dϟƚˈӧRaGd=gGˀё4ՕɊŧȾSԿ/m©²uz²
ՒAmerican chestnutՓjǵӴ3d[\ºɴ?G;OT˦ͧΎʹǋŭ¼ՕͨRʸŴN.f%C. parasitica Tpo³Ւ¦o}po³ՓɊˑRceёϩɐԁӎȑbЩǇȢɐЫ4ï½?ՕΎŞȾa[\̵ƿAf;O4΢dgM/f%]GՕpo³ɊˑRceϳЩƲ͋ѾӮϰYSɊŧȾ4ƱƺAfQPՕϳЩƲSˬӏ4ȦԪjŧ
9M/fOSÏĒΕ΢ѷ4.eՕԥpo³Ɋˑ˗Opo³Ɋˑ˗SEgFgSϳЩƲRΠΚ?MϳЩƲˬɐƹϧSİ΁OǓӵՕˬɐϧİˊϑjѦJG%w·ϹűȾSѣĞсϰ Calcofluor White Rcf C. parasitacaϳЩƲÂw·SǯƞѼǡNTՕԥpo³Ɋˑ˗N.f EP155 ˗Օpo³Ɋˑ˗N.f EP713 ˗Օ
CHV2/EP155 ˗ՕMyRV1/EP155 ˗NEgFgѣĞȠȑ4ƷŎ?M/G%ϳЩƲƹϧSİ΁ǕԽNTՕԥpo³Ɋˑ˗Opo³Ɋˑ˗ԄNՕw·jŶ_ AI ΁İSҮӵRʸɈȂTѷdgQ3JG4Օα13z³u·jŶ_O=gf AS2 ΁İR2/MTՕpo³Ɋˑ˗Sƹ7NҮӵ4́Ǫ?M/G%]GՕˬɐϧİˊSϹˌceՕԥpo³Ɋˑ˗Opo³Ɋˑ˗NTՕϳЩƲƹϧjˬɐAfŰŘϧɐİS̎ͯRƺ5Qә/TѷdgQ3JG%;gdSϹˌceՕpo³ɊˑRceϳЩƲÂSα13z³u·ӵ4ʸɈŔǪ?Օ
;S;O4ΎŞȾOԅӐ?M/fūЫȾ4ίƅ=gG%

Structural changes in fungal cell wall caused by mycovirus infection.
Shoko Mochizuki, Nobuhiro Suzuki* & Shin Kasahara(Miyagi Univ. School of Food, Agric. & Envron. Sci., *IPSR, Okayama Univ.) 87 —P-105ΎŞΟё Aspergillus fumigatus jȞ̍ŎAf¦o}po³ӟêǇSųǓ
ǏɓϾӲԺ 1ՕԿ˵ˢ 1Օ˥ǵѯĜ 2ՕÓÔӋ 1 Ւ1 ŒїƺեΟёŐǋΧσ·¹Օ2 ӀȀƺՓm¢³x³ΏTՕÄR Aspergillus fumigatus RcJMț5ұ;=gf%ųёTŽŷƏ΍Ƀ2cWm´³x¹SŞƔOQf[3ՕģҶRɊˑ?MӳϜŎAf%?3?ŐџͻɝΟёџTοԲ4˪ϊRǪQ7ՕџľНȾёSįͲO/JGƈ԰jɠ1M2eՕʗGQџľSԃΑ4Ƞ7ʻ]gM/f%;Sc0Q̢ͪ½Nɑ&TՕ
A. fumigatus Rǉƞ?ųёjȞ̍ŎAf¦o}po³RΠΚ?ՕʗѸɝΟёџO?MSȺͻjΚɫ?MΧσjѦJM5G%ˀΧσNT;g]NR¦pjͻ/GɊˑǕԽNΎŞȾɛĸňˌjɪK;OjΑѷ?G¦o}po³SӟêǇSģ|¨өĲS̙ǓOՕΎŞȾjɛĸAf¦o}po³ӟêǇSųǓj҉^G%
2 ˗S A. fumigatus ceEgFg˧į?GΎŞȾɛĸňˌjɪK¦o}po³ 2 οS|¨jՕ˹Àá¹
yr·¹ (illumina ΰ Miseq) jͻ/MѾґ?ՕȮdgGөĲRK/M¹·o²o¹¯·2
cW 5RACE ̥jͻ/f;ORcepo³|¨Sģԁj̙Ǔ?G%RdRp (RNA dependent RNA
polymerase)SĄǉԮƦjͻ/G̎ҺϪϽѾˊRceՕ2 οSpo³TOaR;g]NƬźúSQ/ʗοN.
f;O4i3JG%
˹RՕpo³²¹S A. fumigatus İԝ˗ՒKU ˗ՓRpo³|¨S ORF jEgFgȠĸΑͲ=CՕǛÄSȢɋե͹Хӎȑե̴ӋƝНȾեџľНȾQPSѫͲƣՕ2cW¦pYSΎŞȾj̎Һ?G%ˀǋéNTՕ
;gdSѾˊϹˌSƬźjÏǓ?M/f%

Study of mycoviral genes which attenuate virulence of human pathogen, Aspergillus fumigatus
Erika Shishido1, Azusa Takahashi-Nakaguch1, Hiromitu Moriyama2, Tohru Gono1( 1MMRC, Chiba Univ., 2Tokyo Univ. of Agric. & Tech.)

P-106
Aspergillus fumigatus S͹ͺAf´y·Rcf͘ΏҎΑöͻRK/MӫÔԺǀ̖ 1ՕлӴ̱ω 2Օ̖̎˥ɂǇ 2Օȋˋ̺ 2ՕÓÔӋ 1 ՒŒїƺ¸Οё·¹1ՕͺІΧ 2Փ

A. fumigatus Tm¢³x³ΏSÄQŞƔёN.eՕɊˑ¸ʃοS©u¨j΢fG`R˭&QΧσ4
ѦigM/f%ESÂSºKO?MՕǛÄN.fbŊͧª³R2/MՕΎŞёSϳЩѫԦƹϧOEg
jҍқAf´y·4ɊˑԈȯNӳѵQė5j?M/f;O4Ƭź=gM5G%ºʘNՕΟёĐS´y·
4Ɋˑ¸ΎŞȾΑͲR2/MPSc0Qė5j?M/fS3[OkPʣd3RQJM/Q/%E;NՕӄȌ
ɑ&T A. fumigatus S͹ͺAf´y·R͚͝j.MMΎŞȾOSԅieRK/MΧσjѦJM/f%ˀΧσNTՕ;g]NR A. fumigatus S´y·O?MųǓ=gGaSS0IՕfucose RϹűͨ·ȾjɪK
AFL RK/Mҋ?7ғZG%]B 6 KSϧӾϹűԮƦSm§ӯГɺjѦJG AFL jƺбёR2/Möɐ?Օ
ϧӾOSϹűRƷ·4PSc0QȦԪj¿1f3ғZG%ESϹˌ 6 ԮƦS0I 1 ԮƦNTƷ·jĢgfO
·yS͹ͺ4Q7QeՕßS 1 ԮƦNTƷ·jĢgfOՕfucose OSϹű4ƺȊŔǪAf;O4İ3J
G%ͲƞTՕϧӾOSϹű4͘ΏҎΑRPSc0QȦԪj¿1fS3jғZM/fO;hN.f%

The pro-inflammatory reaction of lectin from Aspergillus fumigatus.
Kanae Sakai1, Hiroaki Tateno2, Keiko Hiemori2, Jun Hirabayashi2, Tohru Gonoi1(MMRC, Univ. of Chiba1ՕAIST2)

 88 —-743"ʸ̖Ń ............ 46, 57;

F

Anna Bergs ..... 31, 54

Natasha Savage 31, 54ʸͼξȣ .............. 38

Arthur F. J. Ram .... 16

Nguyen Hieu Hanh 82̸ǿǊЗ . 33, 64, 76,ʸǷǋ .................. 63

Nuo Li ............ 29, 67<
Boris Tefsen ......... 16=
Cees A.M.J.J. van den
Hondel ............. 16̲ӴƟҼ .............. 58ǍѠʫѸ ........ 45, 46

Pei HAN ............... 51ƺԀ͒ ................. 81

Pushpa S Murthy ... 36ÓőǽƟʜǇ ....... 60

ƺũV3f .......... 53H̗ͼďº .............. 82ƺӲĆº .............. 46ΥÔºƽ .............. 57ƺƥȤԩ .............. 36ΥÔɂǇ .............. 40ƺԿ͒ÇÝ .......... 87ΥÔʰǇ .............. 80ƺƮ̺ ................. 63ΥǿԺŗ .............. 67ƺƮƨȎ .............. 61

Υͼď .................. 71ƺ̡Ȏǔ .............. 61

54

Daria Kohler ... 31, 54

G

Rebecca Donnelly . 31,>77ˡǵεʣ .............. 56

Reinhard Fischer ... 31,54?

К̡Χº ........ 34, 78

Ellen Lagendijk ..... 16IΥͼŕË .............. 60

ƺƭ˿ ................. 70@

Scott E. Baker ....... 80ΥͼŒϾ .............. 73ƺϘąº .............. 70ΥŞϯȤӤ ..... 28, 62ƺƭ˽ʧ ........ 28, 62

ΥŞØ .................. 86ƺԲʭǇ ........ 27, 38

Yiming Li ....... 31, 54ǩύŞřą .......... 58

Gero Steinberg ...... 47

̣̬Ȝò ........ 84, 85

Yuji Ishitsuka .. 31, 54̣̬Ȝα .............. 47ǩύŞ̿ .. 69, 74, 75

A̣Ǖ ...................... 58

ǷɦÑ ................. 58ȆǿʠĦ .............. 68ǷӴ˜˴ .............. 48º͖˟Ǉ .............. 43Ƿӧ΢ȝ .............. 49ÔįЄђ .............. 24Ƿ˄ʑԩ .............. 49èѠщӲǇ ........... 71ǷˀЄǇ .............. 71èѠѐº .............. 58ǩǿҬÑ .............. 40ȩ̀ʹƁ .............. 36

ǩǿԬ ........... 45, 46Ģҝȥщ .............. 75ǩǿƃË .............. 46

Ǹ½ſѯ ........ 37, 49

яӴŒη ........ 42, 44Ǹ̀ƺҽ .............. 76ǁͼП ................. 72ǸˀſǇ .............. 64ѠʽОȋ .............. 41

G. Ulrich Nienhaus 31,
54

Helge M. Dietrich . 32,
51

Jéͼǐ˴ .............. 75үʽԣĦ ........ 85, 86ʣΥҧѯ .............. 40

B
Irma van Die ......... 16C̯Ô͑............ 26, 41
̯Ôƺҧ .............. 46
̯Ôђ&Ǖ ... 27, 42,

Jae-Hyuk JANG .... 79

44

Jong Seog AHN .... 79̯Ӵ=O^ .......... 76

Joohae Park .......... 16ԊǬԚʑ .............. 40
ˈʧǀ.................. 36DԊӧӥʺ . 33, 64, 76,

Kenneth S. Bruno .. 80
Kieu Thi Minh Pham........................ 82

EMark Arentshorst .. 1677ǁ˄ ˺ͽ ............ 40ԁͼѯÇ .. 34, 79, 81¼ӴϻǇ .............. 63Бͼď ................. 37ԊӧʍɄ . 26, 27, 29,¼ŞďÑ .. 27, 38, 39

38, 39, 40, 41, 56,¼˄̩ƾ .............. 37

59, 73̐ǙɐԒ .............. 62;ʒȘ˹ .............. 86ԊӧƾѦ .............. 80ɘΡɂº .............. 40

˕ѝ±± .. 26,

ʗÔſр .............. 81ˡ͓σ .................. 60ʗǰӸȋ .............. 78ˡ˄мǇ . 26, 41, 59,э̼ҧÇ ........ 46, 81

 89 —80

44ύŞϴ ........... 35, 87ˤŞȔř .............. 65Ņ͖ʣʜԺ .......... 39

69, 72ͤ̀ͽ÷Ǉ .......... 58ÆĄǺɂ .............. 71ͤǵͶË .............. 55ÆĄȔÇ . 35, 82, 83,

ŅѠԬ ................. 78
ŅѠИ ................. 79ŅѠΛ˴ .............. 79ŅѠԚƵ .. 28, 62, 66
 . 29, 31, 32,
54, 55, 67, 69, 7484
˞ͼъ............ 46, 81ǩ̗щʣ . 26, 41, 59,80

ӶǇΟË .............. 76ӶǇęȋ .. 28, 62, 66ġͰƨºʺ .... 85, 86ӽćԿȹ ........ 79, 81ǩǺɏÝ ........ 32, 55

ÍÔğȣ .............. 65ǩǾ̷.................. 78˫ӴŢԺ .............. 48

ǩԅŕË .............. 61яӴŒη .............. 27ǩͰϯá .............. 83̞ű̽ ................. 56ȫѠ˽Ķ ........ 58, 65

ǿ¼ſЗ .............. 40ÓÔӋ ........ 65, 88ǿũнȋ .............. 53ǩˋɦƍ .............. 57ǿũĽů .. 30, 72, 86ǩˋƃƽ . 28, 29, 31,ǿϊʠ ................. 84

32, 54, 55, 62, 67,ǿ˄ʰ˴ .............. 60

69, 74ǿˀӑ ........... 65, 70

ÓżŌË . 30, 33, 37,ǿˀΟË .............. 86

43, 52, 58, 62, 66,

ģʰɹ ................. 77

68, 70ǩ˥ͽЕǇ .......... 40ӄѠʩȣ .. 27, 42, 44

ѐǿǠŭ ........ 45, 46
ѐԄԒȹ .. 41, 52, 53
ŏǿ̠ɂ .............. 70ÜӴŢЂ .............. 37ƯǱȍ˴ .. 69, 74, 75ъˀÚҼ .............. 71ǏɓϾӲԺ ........... 88ϛƮʟϫ .............. 58
ǺϮ ...................... 45̽̒ȹĄ .............. 24ȹ̒ěØ .. 28, 62, 66
ԨӻԬ ............ 26, 44
ȏůӥƾ .............. 56
ΓΥӑ .................. 76Γơɏω ........ 61, 64
ȹ̧ę .................. 55
Ӷӹˇ ...... 49, 50, 51ʗҝǫȜ . 30, 33, 37,
43, 52, 66, 68, 70ʗǙºͿ ........ 26, 41ՎѠÚ.................. 78ŏˀŌV; ... 32, 41,ӫÔԺǀ̖ .... 65, 88

42, 49, 50, 51, 52,ơũ˿............ 83, 84ԇˀՆѦ .............. 45όħӗԙ . 57, 63, 68,
71, 72όǿў ........... 58, 65
ό½ĦͿ ........ 31, 54όˀƺŸ ........ 48, 49ͼáʰŭ .............. 65ƹͼń͹ .............. 53лӴ̱ω .............. 88ͼÂɉǇ .............. 49ͼÂɦʾ .. 27, 38, 39
ͼÂŒǦ .. 47, 84, 85ͼÂͷȃ . 30, 33, 37,
43, 52, 66, 68, 70
ͼÂŉ̑ .. 32, 50, 51
ͼÂԑǇ ........ 34, 81ͼӣȜ̊ ........ 27, 38
ҝĆ̠ ..... 30, 72, 86
ͼÇćę .............. 63ͰГǫȳ .............. 65˂ǵнȋ .............. 70ͰӴǊº .. 26, 41, 80ӷʽτƼ .............. 37'ӷʽП ............ 36, 65
ӷʽąȜ ........ 35, 87
ӷʽє .................. 62ΦǿȻȎ .............. 19͙ҝԬº .. 30, 72, 86%͖ǭъЕ .............. 87ӶĚŝ ..... 27, 38, 39ơˀѯº .............. 76&

Ӷӹˇ ........... 32, 42ñÆԄƃŭ .......... 46ԿǭſǕ .............. 85ʽ˄Ο29, 31, 32, 54,˷ҝщ̠ ........ 45, 46

Կʽȸ .................. 2555, 67, 69, 74ϏćΛË ........ 27, 44Կ½εʧ .............. 65ñѠȹρ .............. 76

Կ˵ˢ .................. 88ñѠƺҧ .............. 40Կ˵ăÑ .............. 79˨ͼͷρ .............. 61ñѠʧђ .............. 69Կ˵ɌƼӦ ........... 40

˨ˀɏº ........ 36, 53ñӴěʩ .............. 70Կ˵ȵ 27, 38, 39, 40

ˁʘȔѯ .............. 39ՃǺ˽̱ .............. 60

Հ˵ȵ ............ 26, 44ȀѠ÷ӤǇ .......... 62Կѷҏº .............. 40. 29, 30, 67,ԿҝΛ˴ . 34, 71, 78,Կ˓ÕͽЕ .......... 63$ðͼŕË ........ 84, 85"ŏįԙ͹ ........ 47, 85

53, 63ƯӴЗÛ .............. 61ȹͼ̫Ý .. 69, 74, 75!

ŪǼĶϫ .............. 57



80

#

 90 —ȟʖˆ ................. 43
Œáę ................. 73(ƮǼſ÷Ǉ .... 49, 50
ƮŞ˽ă .............. 36˒˦ǫȹ ........ 85, 86
ӂÔԚ ................. 72ǧԻѯҏ .............. 39
ƫ̱Ǉ ..... 27, 42, 44)
Ǣħѯҧ .............. 39Ǣ½Ԓƽ .............. 61
o µ ................ 57*ƪļƟò .............. 39ī˳ҧɐ .............. 40͂ÆƠʊ̘ .......... 36ɓҝĞȋ .............. 60ˋʟϫ............ 32, 55

ļˋ˽Ȝ ........ 28, 62Ƹǵřщ .............. 36ŞͼҬ............ 35, 82

ˠǭăÝ .............. 80ʧѷԒʑ .............. 78ˠǭăÝ .............. 71+Â̝ǅÛ ........ 28, 59

œˀǒ .................. 47/΀ͼԚÇ . 26, 41, 59,Â͓ǀЕ ........ 34, 78

̖̎˥ɂǇ .......... 88ÂǺʧϲ ........ 39, 73

˯ũĽȹ .............. 38ÂǾòº .............. 74˯ũѯ˹Ӧ .......... 47ÂӂҔȋ ........ 45, 46ȋ̝ƺ˴ .............. 74ˉ˄Ժђ .............. 40ԁӴȈЕ .. 26, 41, 59

ȋˋ̺.................. 88Ãǵ͒º . 32, 42, 49,ÂӴǐҷ .............. 39ȋˉρÅф .......... 40Â˄ȥȣ .............. 60Ȗ͓ɦȄ .............. 81Â˄ԘÛ .............. 66Â˄ȍǐ .............. 21080ˉͼûƺ . 33, 64, 76,
77

50, 516ǵȢ̫ȋ . 57, 63, 68,
71, 72ǵǿϹ ................. 73ǵǼŻȋ .............. 68ǵ½ìԙ .............. 40
ǵͼĆ ..... 26, 36, 44
ǵ˙ČǇ .............. 80ǵˀŕ ................. 46ǵˀψË ........ 28, 62

73»̰ɉ .................. 80ӓÍИƼ ........ 30, 72
ԟΟȜ ................. 69ÂǱʐƢ ........ 75, 82̹ͼŭЕ ........ 83, 84

̒ҝ̠ ............ 26, 44

ÂǵΟͽЕ ... 29, 56,

δͼ̩Æ ........ 61, 64»ҝԒǐ .............. 528δԄ̩Ç .............. 56»˵Ԓω ........ 64, 77˲Ρ÷ǀ .............. 75̓ǵɂЕ .............. 38δˀǋ.................. 40Їǿѯр .............. 56Ųǿřʑ .............. 55

ɐǿɂ ................. 81ѠÔӥԙ .............. 49ǗǿɦË .............. 63ѠǷʰĻ .............. 56

Ųͼҏ ................. 60ǗǼſȜ .............. 76Ñβ̩ƨ .............. 65ŲѷƉ 29, 56, 59, 73

ǗǼǍǥ .. 28, 59, 76

Ų˄Ї ........... 30, 66

49˄ƤĤщ .............. 40

чÔʱ ..... 27, 42, 44

˄ũě .................. 48

Эˀʋȍ ........ 33, 77˄ӴɎǀ .............. 81͂ӧʩ ................. 625͂Ӂƚʮ .............. 2473,Ñʇ ăω ............ 40Ñ͖ȤǇ .............. 24Ѵ˄ՋӲ̖ .......... 87пǵ.B^ .... 31, 54Ӵ˄Ɗȍ .............. 58.

ŪǿďƼӦ ... 29, 56,
73

1
ʥ̱ж.................. 57

яŞ̺ ................. 78ƩħѯÇ .. 55, 56, 57

ʻʷИǇ ........ 35, 87ѕŞƺα .. 56, 65, 70ˀͼ¿º ........ 28, 59

ʻʷՋѪ ........ 28, 62ԁҝǿՖƥγǇ ... 68
΃Â;B1 .......... 48

ъʽЕ˴ .............. 782ˀǵԿȍ .. 34, 79, 81

ι̫Ñ 21, 27, 42, 44ļͼºѦ .............. 74˥ͼǠÛ .............. 71ʟǿуòѓ .......... 73ļͼ̱ 57, 63, 68, 71˥ǵѯĜ .............. 88

 91 —͂Ӣ̩α .............. 36͂ӁԒȍ .............. 58͂ӢѯË .............. 61͂ӢαӲϾ .......... 40ϩͪёİǇ͹ͧǋΧσé éĻ
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） 92 —2*6

+(!/0:1é  ԁ
小林 哲夫

名古屋大学大学院 生命農学研究科

ӔƌǄƂԊӧ ʍɄ

ˈŏƺǋƺǋԍӀǋΧσθʸǷ ǋՒȓŋɣȡՓˈÙƺǋƺǋԍӀǋ͹žθǋΧσθÓőǽ ƟʜǇˈÙƺǋƺǋԍӀǋ͹žθǋΧσθǩύŞ ̿

ԁǷəѧθǋƺǋ͹ͧϪŅѠ ԚƵՒéҁɣȡՓŴƥƺǋӀǋӧǿũ ĽůՒȎƬɣȡՓƺԇȐχƺǋƺǋԍ͹ž͸ưθǋΧσθñӴ ěʩ

Ӷ̝Ȁ˩ƺǋ|¨͹ͧȀǋΧσɕԿʽ ȸ¤o¨ «·˗ȚéΰΧσԃΑӧԿӴ ЗǊÙӨƺǋƺǋԍӀǋΧσθԿҝ Λ˴

ϒ̧ƺǋ͹ž͸ưθǋΧσθѴ˄ ՋӲ̖ͫχѦʊ̥ÛӀ˩͹ͧҪ͈Χσɕι ̫Ñʷ˜Ī˗ȚéΰІűΧσɕǵȢ ̫ȋՒЊԛɣȡՓˈÙӀȀƺǋƺǋԍӀǋΧσԍǵͼ ĆéҁΘ˔όħ ӗԙ

ͫχѦʊ̥ÛӫԲІűΧσɕˈÙӀȀƺǋƺǋԍӀǋΧσԍ 93 —2*6;

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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 94 —25th anniversary of Japan Society For
Molecular Biology of Filamentous Fungi
基調講演
北北本勝ひこ 先⽣生

特別講演
別府 輝彦 先⽣生記念念講演

町⽥田 雅之先⽣生
五味 勝也 先⽣生
⼭山⽥田 修 先⽣生
森川 康 先⽣生
秦 洋⼆二 先⽣生⻑⾧長⽥田 裕之 先⽣生

第36回例例会
同時開催
奨励賞講演
技術賞講演
（12⽉月末まで
公募予定）

講演会は参加無料料、懇親会費⽤用は後⽇日ご連絡の予定です。
詳しくは以下の連絡先(URL)をご覧ください。
http://fungi.mysterious.jp/MAIN-J/Welcome.html

期⽇日：平成27年年6⽉月19⽇日（⾦金金）会場：北北とぴあ つつじホール
東京都北北区王⼦子1丁⽬目11番地1号

お問い合わせ：岩下和裕、織⽥田 健(酒類総合研究所内 ⽷糸状菌遺伝⼦子研究会事務局)
広島県東広島市鏡⼭山3-7-1
Tel: 082-420-0824
E-mail: info@fungi.mysterious.jp

第 14 回糸状菌分子生物学コンファレンス要旨集

平成 26 年 10 月 20 日 印刷
平成 26 年 10 月 20 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