中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
MutL associates with Escherichia coli RecA and inhibits its ATPase activity

文献类型:期刊论文

作者Zhang, Min ; Zhou, Ying ; Li, Tao ; Wang, Hailin ; Cheng, Fang ; Zhou, Yafeng ; Bi, Lijun ; Zhang, Xian-En
刊名Biochemistry & Molecular Biology; Biophysics
出版日期2012
卷号517期号:2页码:98-103
关键词RecA MutL Homologous recombination Protein interaction
ISSN号0003-9861
中文摘要Different DNA repair systems are known to cooperate to deal with DNA damage. However, the regulatory role of the cross-talk between these pathways is unclear. Here, we have shown that MutL, an essential component of mismatch repair, is a RecA-interacting protein, and that its highly conserved N-terminal domain is sufficient for this interaction. Surface plasmon resonance and capillary electrophoresis analyses revealed that MutL has little effect on RecA-ssDNA filament formation, but dose down-regulate the ATPase activity of RecA. Our findings identify a new role for MutL, and suggest its regulatory role in homologous recombination. (C) 2011 Published by Elsevier Inc.
WOS记录号WOS:000299146000002
公开日期2014-11-27
源URL[http://ir.rcees.ac.cn/handle/311016/8069]  
专题生态环境研究中心_环境化学与生态毒理学国家重点实验室
推荐引用方式
GB/T 7714
Zhang, Min,Zhou, Ying,Li, Tao,et al. MutL associates with Escherichia coli RecA and inhibits its ATPase activity[J]. Biochemistry & Molecular Biology; Biophysics,2012,517(2):98-103.
APA Zhang, Min.,Zhou, Ying.,Li, Tao.,Wang, Hailin.,Cheng, Fang.,...&Zhang, Xian-En.(2012).MutL associates with Escherichia coli RecA and inhibits its ATPase activity.Biochemistry & Molecular Biology; Biophysics,517(2),98-103.
MLA Zhang, Min,et al."MutL associates with Escherichia coli RecA and inhibits its ATPase activity".Biochemistry & Molecular Biology; Biophysics 517.2(2012):98-103.

入库方式: OAI收割

来源:生态环境研究中心

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