Structural study of translesion DNA polymeraseζ/REV1 complex

点击翻译按钮获取中文摘要

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.