Structural insights into the assembly of human translesion polymerase complexes  

作　　者：Wei Xie Xuan Yang Min Xu Tao Jiang 

机构地区：[1]National Laboratory of Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences,15 Datun Road,Chaoyang District,Beijing 100101,China [2]The Graduate University of Chinese Academy of Sciences,19A Yuquan Road,Shijingshan District,Beijing 100039,China

出　　处：《Protein & Cell》2012年第11期864-874,共11页蛋白质与细胞（英文版）

基　　金：supported financially by the National Basic Research Program(973 Program)(No.2011CB910302);the National Natural Science Foundation of China(Grant Nos.31025009,31021062 and 31200558).

摘　　要：In addition to DNA repair pathways,cells utilize translesion DNA synthesis(TLS)to bypass DNA lesions during replication.During TLS,Y-family DNA polymerase(Polη,Polκ,Polιand Rev1)inserts specific nucleotide opposite preferred DNA lesions,and then Polζ consisting of two subunits,Rev3 and Rev7,carries out primer extension.Here,we report the complex structures of Rev3-Rev7-Rev1^(CTD) and Rev3-Rev7-Rev1^(CTD)-Polκ^(RIR).These two structures demonstrate that Rev1^(CTD) contains separate binding sites for Polκand Rev7.Our BIAcore experiments provide additional support for the notion that the interaction between Rev3 and Rev7 increases the affinity of Rev7 and Rev1.We also verified through FRET experiment that Rev1,Rev3,Rev7 and Polκ form a stable quaternary complex in vivo,thereby suggesting an efficient switching mechanism where the“inserter”polymerase can be immediately replaced by an“extender”polymerase within the same quaternary complex.

关 键 词：translesion DNA synthesis Rev1 Polκ Polζ complex structure 

分 类 号：F55[经济管理—产业经济]