Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair

被引:24
|
作者
Hingorani, Manju M. [1 ]
机构
[1] Wesleyan Univ, Middletown, CT 06459 USA
基金
美国国家科学基金会;
关键词
Mismatch repair; MutS; MutL; ATPase mechanism; Transient kinetics; ESCHERICHIA-COLI MUTS; C-TERMINAL DOMAIN; DNA MISMATCH; CONFORMATIONAL-CHANGES; CRYSTAL-STRUCTURE; BIOCHEMICAL-ANALYSIS; NUCLEOTIDE-BINDING; SLIDING CLAMP; PROTEIN MUTS; HMUTS-ALPHA;
D O I
10.1016/j.dnarep.2015.11.017
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
The focus of this article is on the DNA binding and ATPase activities of the mismatch repair (MMR) protein, MutS-our current understanding of how this protein uses ATP to fuel its actions on DNA and initiate repair via interactions with MutL, the next protein in the pathway. Structure-function and kinetic studies have yielded detailed views of the MutS mechanism of action in MMR. How MutS and MutL work together after mismatch recognition to enable strand-specific nicking, which leads to strand excision and synthesis, is less clear and remains an active area of investigation. (C) 2015 Elsevier B.V. All rights reserved.
引用
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页码:24 / 31
页数:8
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