Molecular mechanisms for modification of carbon catabolite repressors and sugar transporters in filamentous fungi

2016 Fiscal Year Final Research Report

• Project/Area Number: 25292044
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Applied microbiology
• Research Institution: Tohoku University
• Principal Investigator: GOMI KATSUYA 東北大学, (連合)農学研究科(研究院), 教授 (60302197)
• Co-Investigator(Renkei-kenkyūsha): SHINTANI TAKAHIRO 東北大学, 大学院農学研究科, 准教授 (70374973)
• 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
• Project Period (FY): 2013-04-01 – 2017-03-31
• 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

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.

Free Research Field

応用微生物学