The interaction of DNA mismatch repair proteins with human exonuclease I

被引：129

作者：

Schmutte, C ^{[1
]}

Sadoff, MM ^{[1
]}

Shim, KS ^{[1
]}

Acharya, S ^{[1
]}

Fishel, R ^{[1
]}

机构：

[1] Thomas Jefferson Univ, Kimmel Canc Ctr, Genet & Mol Biol Program, Dept Microbiol & Immunol, Philadelphia, PA 19107 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2001年 / 276卷 / 35期

关键词：

D O I：

10.1074/jbc.M102670200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Exonucleolytic degradation of DNA is an essential part of many DNA metabolic processes including DNA mismatch repair (MMR) and recombination. Human exonuclease I (hExoI) is a member of a family of conserved 5' --> 3' exonucleases, which are implicated in these processes by genetic studies. Here, we demonstrate that hExoI binds strongly to hMLH1, and we describe interaction regions between hExoI and the MMR proteins hMSH2, hMSH3, and hMLH1. In addition, hExoI forms an immunoprecipitable complex with hMLH1/hPMS2 in vivo. The study of interaction regions suggests a biochemical mechanism of the involvement of hExoI as a downstream effector in MMR and/or DNA recombination.

引用

页码：33011 / 33018

页数：8

共 61 条

[1] Crystal structure and ATPase activity of MutL: Implications for DNA repair and mutagenesis [J].