Elucidation of protein secreting mechanisms of filamentous fungi by the comparative genomic analysis
Project/Area Number |
23603002
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biomass energy
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Research Institution | Nagaoka University of Technology |
Principal Investigator |
|
Project Period (FY) |
2011 – 2013
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
|
Keywords | 糸状菌 / 比較ゲノム解析 / セルロース / セルラーゼ |
Research Abstract |
The cellulolytic filamentousfungus Trichoderma reesei secrets a tremendous amount of proteins and almost all of these proteins are cellulases and hemicellulases. Therefore, T. reesei is an ideal model organism to understand protein secretion mechanism of filamentous fungi. The goal of this study is to understand cellulase production mechanisms of T. reesei through comparative genomic analysis of a cellulase hyper-producing mutant lineage developed in Japan. After sequencing the genome of T. reesei mutants, by a Next-Generation Sequencer, a number of single nucleotide polymorphisms (SNPs) were identified. We focused on three mutated genes which are cre1 encoding the carbon catabolite repressor, bglr encoding transcriptional activator of intracellular beta-glucosidase, and bgl2 encoding major intracellular beta-glucosidase BGLII. From gene disruption and complementation of mutated nucleotide, these SNPs were found to be responsible for increased cellulase production.
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Report
(4 results)
Research Products
(41 results)
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[Journal Article] Single Nucleotide Polymorphism Analysis of a <i>Trichoderma reesei</i> Hyper-Cellulolytic Mutant Developed in Japan2013
Author(s)
Porciuncula JD, Furukawa T, Mori K, Shida Y, Hirakawa H, Tashiro K, Kuhara S, Nakagawa S, Morikawa Y, Ogasawara W
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Journal Title
Bioscience, Biotechnology, and Biochemistry
Volume: 77
Issue: 3
Pages: 534-543
DOI
NAID
ISSN
0916-8451, 1347-6947
Related Report
Peer Reviewed
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