| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2010: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| 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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