M
Motoaki Sano
Researcher at National Institute of Advanced Industrial Science and Technology
Publications - 38
Citations - 2316
Motoaki Sano is an academic researcher from National Institute of Advanced Industrial Science and Technology. The author has contributed to research in topics: Aspergillus oryzae & Gene. The author has an hindex of 12, co-authored 35 publications receiving 2188 citations. Previous affiliations of Motoaki Sano include National Institute of Technology and Evaluation & Kanazawa Institute of Technology.
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Journal ArticleDOI
Genome sequencing and analysis of Aspergillus oryzae
Masayuki Machida,Kiyoshi Asai,Motoaki Sano,Toshihiro Tanaka,Toshitaka Kumagai,Goro Terai,Goro Terai,Ken Ichi Kusumoto,Toshihide Arima,Osamu Akita,Yutaka Kashiwagi,Keietsu Abe,Katsuya Gomi,Hiroyuki Horiuchi,Katsuhiko Kitamoto,Tetsuo Kobayashi,Michio Takeuchi,David W. Denning,James E. Galagan,William C. Nierman,Jiujiang Yu,David B. Archer,Joan W. Bennett,Deepak Bhatnagar,Thomas E. Cleveland,Natalie D. Fedorova,Osamu Gotoh,Hiroshi Horikawa,Akira Hosoyama,Masayuki Ichinomiya,Rie Igarashi,Kazuhiro Iwashita,Praveen R. Juvvadi,Masashi Kato,Yumiko Kato,Taishin Kin,Akira Kokubun,Hiroshi Maeda,Noriko Maeyama,Jun-ichi Maruyama,Hideki Nagasaki,Tasuku Nakajima,Ken Oda,Kinya Okada,Ian T. Paulsen,Kazutoshi Sakamoto,Toshihiko Sawano,Mikio Takahashi,Kumiko Takase,Yasunobu Terabayashi,Jennifer R. Wortman,Osamu Yamada,Youhei Yamagata,Hideharu Anazawa,Yoji Hata,Yoshinao Koide,Takashi Komori,Yasuji Koyama,Toshitaka Minetoki,Sivasundaram Suharnan,Akimitsu Tanaka,Katsumi Isono,Satoru Kuhara,Naotake Ogasawara,Hisashi Kikuchi +64 more
TL;DR: Specific expansion of genes for secretory hydrolytic enzymes, amino acid metabolism and amino acid/sugar uptake transporters supports the idea that A. oryzae is an ideal microorganism for fermentation.
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System-level identification of transcriptional circuits underlying mammalian circadian clocks.
Hiroki R. Ueda,Satoko Hayashi,Wenbin Chen,Motoaki Sano,Masayuki Machida,Yasufumi Shigeyoshi,Masamitsu Iino,Seiichi Hashimoto +7 more
TL;DR: The results indicate that circadian transcriptional circuits are governed by two design principles: regulation of E/E′ boxes and RevErbA/ROR binding elements follows a repressor-precedes-activator pattern, resulting in delayed transcriptional activity, whereas regulation of DBP/E4BP4 binding elements following a repression-antiphasic-to-activators mechanism, which generates high-amplitude transcriptionalactivity.
Journal ArticleDOI
Transcriptional analysis of genes for energy catabolism and hydrolytic enzymes in the filamentous fungus Aspergillus oryzae using cDNA microarrays and expressed sequence tags.
Hiroshi Maeda,Motoaki Sano,Yutaka Maruyama,Takeki Tanno,Takeshi Akao,Yoshiteru Totsuka,Misako Endo,Rumi Sakurada,Youhei Yamagata,Masayuki Machida,Osamu Akita,Fumihiko Hasegawa,Keietsu Abe,Katsuya Gomi,Tasuku Nakajima,Yasutaka Iguchi +15 more
TL;DR: The wheat-bran culture gave the richest gene expression profile of hydrolytic enzymes and the lowest expression levels of catabolic genes (EMP, TCA) among the three media tested, suggesting that A. oryzae uses both EMP and TCA for glucose metabolism under AC conditions.
Journal ArticleDOI
Analysis of Expressed Sequence Tags from the Fungus Aspergillus oryzae Cultured Under Different Conditions
Takeshi Akao,Motoaki Sano,Osamu Yamada,Terumi Akeno,Kaoru Fujii,Kuniyasu Goto,Sumiko Ohashi-Kunihiro,Kumiko Takase,Makoto Yasukawa-Watanabe,Kanako Yamaguchi,Yoko Kurihara,Jun-ichi Maruyama,Praveen R. Juvvadi,Akimitsu Tanaka,Yoji Hata,Yasuji Koyama,Shotaro Yamaguchi,Noriyuki Kitamoto,Katsuya Gomi,Keietsu Abe,Michio Takeuchi,Tetsuo Kobayashi,Hiroyuki Horiuchi,Katsuhiko Kitamoto,Yutaka Kashiwagi,Masayuki Machida,Osamu Akita +26 more
TL;DR: Data showed that consideration of culture grown under various conditions as cDNA sources enabled efficient collection of ESTs, and contig sequences were compared with sequence sets in eukaryotic orthologous groups (KOGs), and classified into the KOG functional categories.
Journal ArticleDOI
Plasmid-Encoded asp Operon Confers a Proton Motive Metabolic Cycle Catalyzed by an Aspartate-Alanine Exchange Reaction
Keietsu Abe,Keietsu Abe,Fumito Ohnishi,Kyoko Yagi,Tasuku Nakajima,Takeshi Higuchi,Motoaki Sano,Masayuki Machida,Rafiquel Sarker,Peter C. Maloney +9 more
TL;DR: The asp operon confers a proton motive metabolic cycle consisting of the electrogenic aspartate-alanine antiporter and the as partate decarboxylase, which keeps intracellular levels of alanine, the countersubstrate for aspartates, high.