2011 Fiscal Year Final Research Report
Structural study of translesion DNA polymeraseζ/REV1 complex
Project/Area Number |
22770109
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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Research Institution | Yokohama City University |
Principal Investigator |
HASHIMOTO Hiroshi 横浜市立大学, 生命ナノシステム科学研究科, 助教 (40336590)
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Project Period (FY) |
2010 – 2011
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Keywords | X線結晶解析 |
Research Abstract |
REV1, REV3 and REV7 are pivotal proteins in translesion DNA synthesis that allows to continue DNA synthesis even in the presence of DNA damage. REV1 and REV3 are error-prone DNA polymerases. REV7 interacts with both polymerases, thereby acts as an adaptor protein that functionally links those polymerases. The ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment was successfully crystallized. The crystals belong to the space group of P3_121 with the cell-dimension of a=b=74.7, c=124.5 Å and・=120°. Electron density map obtained from molecular replacement method using REV7-REV3 complex as a search model clearly shows that the REV1 C-terminal domain adopts a four-helices bundle structure.
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[Presentation] Structure of REV7 in complex with a REV3 fragment and structural implication of the interaction between DNA polymeraseζ and REV12011
Author(s)
Hiroshi Hashimoto, Kodai Hara, Yoshiki Murakumo, Shunsuke Kobayashi, Toshiaki Kogame, Satoru Unzai, Satoko Akashi, Shunichi Takeda, Toshiyuki Shimizu, Mamoru Sato
Organizer
NH Grand Hotel Krasnapolsky
Place of Presentation
Amsterdam, Netherlands
Year and Date
20110607-09
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