Understanding of molecular mechanism of the assembly of two RecA homologs, Rad51 and Dmc1
| Project/Area Number |
23247029
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Molecular biology
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| Research Institution | Osaka University |
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Principal Investigator |
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| Project Period (FY) |
2011-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥48,750,000 (Direct Cost: ¥37,500,000、Indirect Cost: ¥11,250,000)
Fiscal Year 2013: ¥14,300,000 (Direct Cost: ¥11,000,000、Indirect Cost: ¥3,300,000)
Fiscal Year 2012: ¥14,820,000 (Direct Cost: ¥11,400,000、Indirect Cost: ¥3,420,000)
Fiscal Year 2011: ¥19,630,000 (Direct Cost: ¥15,100,000、Indirect Cost: ¥4,530,000)
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| Keywords | 組換え / 減数分裂 / ゲノム安定化 / Rad51 / Dmc1 / 染色体 / RecAホモログ |
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| Outline of Final Research Achievements |
During recombination, homology search between two DNA molecules is a key reaction which is mediated by the RecA homolog Rad51 during mitosis. On the other hand, homology search in meiotic recombination is catalyzed by a collaborative action of two RecA homolog, Rad51 and Dmc1. Both Rad51 and Dmc1 form a filament on the single-stranded DNAs which is regulated in a positive and negative way. We identified a new protein complex containing Psy3, Csm2, Shu1 and Shu2 for Rad51 assembly. We determined a crystal structure of a core component of this complex, Psy3-Csm2. Surprisingly, Psy3-Csm2 shows a structural similarity to Rad51 dimer, although there is little sequence similarity between the proteins. Based on the structure, we propose how the Psy3-Csm2 promotes Rad51 filament on the DNA. This is very novel finding to understand molecular mechanism on how Rad51 mediators facilitate Rad51 filament formation.
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] A new protein complex promoting the assembly of Rad51 filaments.2013
Author(s)
Sasanuma H., Tawaramoto M. S., Lao J. P., Hosaka H., Sanda E., Suzuki M., Yamashita E., Hunter N., Shinohara M., Nakagawa A., Shinohara A.
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Journal Title
Nat. Commun.
Volume: 4
Issue: 1
Pages: 1676-1676
DOI
Related Report
Peer Reviewed
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[Journal Article] The small GTPase Rab5 homologue Ypt5 regulates cell morphology, sexual development, iron-stress response and vacuolar formation in fission yeast.2013
Author(s)
Tsukamoto, Y., Katayama, C., Shinohara M., Shinohara, A., Maekawa, S. and Miyamoto M.
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Journal Title
Biochem. Biophys. Res Commun.
Volume: 441
Issue: 4
Pages: 867-872
DOI
Related Report
Peer Reviewed
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