Functional analysis of a codon-independent release factor YaeJ
Project/Area Number |
23570205
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Molecular biology
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Research Institution | Gunma University |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
IMENO Hyota 弘前大学, 農学生命科学部, 教授 (80208785)
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Project Period (FY) |
2011 – 2013
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Project Status |
Completed (Fiscal Year 2013)
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Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2011: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
Keywords | 翻訳停滞解消因子 / リボソームレスキュー / 翻訳 / リボソーム / YaeJ |
Research Abstract |
The YaeJ protein is a codon-independent release factor with peptidyl-tRNA hydrolysis (PTH) activity, and functions as a stalled-ribosome rescue factor in Escherichia coli. To identify residues required for YaeJ function, we performed mutational analysis for in vitro PTH activity towards rescue of ribosomes stalled on a nonstop mRNA, and for ribosome binding efficiency. We focused on residues conserved among bacterial YaeJ proteins. While no YaeJ-specific residues important for PTH activity occur in the structured GGQ domain, Arg118, Leu119, Lys122, Lys129, and Arg132 in the following C-terminal extension were required for PTH activity. All of these residues are completely conserved among bacteria. Single amino acid substitutions for each of these residues significantly decreased ribosome binding efficiency. These biochemical findings provide clues to understanding how YaeJ enters the A-site of stalled ribosomes.
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Report
(4 results)
Research Products
(33 results)
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[Journal Article] Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ.2014
Author(s)
Kogure, H., Handa, H., Nagata, M., Kanai, N., Guntert, P., Kubota, K., Nameki, N.
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Journal Title
Nucleic Acids Research
Volume: 42
Issue: 5
Pages: 3152-3163
DOI
Related Report
Peer Reviewed
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[Journal Article] Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf652012
Author(s)
Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S., Nameki, N.
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Journal Title
Proteins
Volume: 80
Pages: 2629-2642
Related Report
Peer Reviewed
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[Journal Article] Inhibitory effects of choline-O-sulfate on amyloid formation of human islet amyloid polypeptide.2012
Author(s)
Hagihara, M., Takei, A., Ishii, T., Kubota, K., Wakamatsu, K., Nameki, N.
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Journal Title
FEBS Open Bio
Volume: 2
Issue: 1
Pages: 20-25
DOI
Related Report
Peer Reviewed
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[Journal Article] Solutionstructure and siRNA-mediated knockdown analysis of the mitochondorial disease-related protein C12orf652012
Author(s)
Kogure H, Hikawa Y, Hagihara M, Tochio N, Koshiba S, Inoue Y, Guntert P, Kigawa, T, Yokoyama S, and Nameki N
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Journal Title
Proteins
Volume: 80
Issue: 11
Pages: 2629-2642
DOI
Related Report
Peer Reviewed
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[Book] Encyclopedia of Systems Biology2013
Author(s)
Nameki, N., Someya, T., Kawai, G.
Publisher
Springer New York (著書, 分担) Translational control with small RNAs. In : Dubitzky W, Wolkenhauer O, Cho K-H, Yokota H. (editors)
Related Report
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