| Project/Area Number |
25292044
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Tohoku University |
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Principal Investigator |
GOMI KATSUYA 東北大学, (連合)農学研究科(研究院), 教授 (60302197)
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| Co-Investigator(Renkei-kenkyūsha) |
SHINTANI TAKAHIRO 東北大学, 大学院農学研究科, 准教授 (70374973)
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| Research Collaborator |
TANAKA MIZUKI 東北大学, 大学院農学研究科, 博士研究員
ICHINOSE SAKURAKO 東北大学, 大学院農学研究科, 大学院生
MATSUURA YUKA 東北大学, 大学院農学研究科, 大学院生
TADA HINAKO 東北大学, 大学院農学研究科, 大学院生
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| Project Period (FY) |
2013-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥16,120,000 (Direct Cost: ¥12,400,000、Indirect Cost: ¥3,720,000)
Fiscal Year 2015: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2014: ¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2013: ¥7,930,000 (Direct Cost: ¥6,100,000、Indirect Cost: ¥1,830,000)
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| Keywords | 糸状菌 / 遺伝子発現制御 / カーボンカタボライト抑制 / 糖トランスポーター / エンドサイトーシス / ユビキチン化 / アミラーゼ生産 / 転写因子 / 膜輸送体 / ユビキチン / アレスチン / 細胞内局在 / トランスポーター |
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| Outline of Final Research Achievements |
The abundance of the carbon catabolite repressor CreA was reduced after incubation in the maltose and xylose media that induce amylase and xylanase gene expression in A. oryzae. Subcellular localization analysis suggested that maltose and xylose stimulated export of CreA from the nucleus to the cytoplasm and mutation of a putative nuclear export signal resulted in nuclear retention and significant stabilization of CreA. CreA protein level was reduced by disruption of creB and creC, both of which encode the deubiquitinating enzyme complex, but not affected by disruption of creD encoding an arrestin-like protein.
CreD was involved in glucose-induced endocytosis of maltose permease and carbon catabolite de-repression of amylase gene expression in A. oryzae. Dephosphorylation of CreD was required for carbon catabolite de-repression triggered by the disruption of creB; a combination of the phosphorylation-defective mutation of CreD and creB disruption improved amylolytic enzyme production.
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