Steady-state ATPase activity of E-coli MutS modulated by its dissociation from heteroduplex DNA
SCIE
SCOPUS
- Title
- Steady-state ATPase activity of E-coli MutS modulated by its dissociation from heteroduplex DNA
- Authors
- Heo, SD; Cho, M; Ku, JK; Ban, C
- Date Issued
- 2007-12-14
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Abstract
- The ability of MutS to recognize mismatched DNA is required to initiate a mismatch repair (MMR) system. ATP binding and hydrolysis are essential in this process, but their role in MMR is still not fully understood. In this study, steady-state ATPase activities of MutS from Escherichia coli were investigated using the spectrophotometric method with a double end-blocked heteroduplex containing gapped bases. The ATPase activities of MutS increased as the number of gapped bases increased in a double end-blocked heteroduplex with 2-8 gapped bases in the chain, indicating that MutS dissociates from DNA when it reaches a scission during movement along the DNA. Since movement of MutS along the chain does not require extensive ATP hydrolysis and the ATPase activity is only enhanced when MutS dissociates from a heteroduplex, these results support the sliding clamp model in which ATP binding by MutS induces the formation of a hydrolysis-independent sliding clamp. (C) 2007 Elsevier Inc. All rights reserved.
- Keywords
- MutS; steady-state ATPase activity; spectrophotometric method; double end-blocked heteroduplex; gapped DNA; MISMATCH REPAIR; HMUTS-ALPHA; TRANSLOCATION MECHANISM; SLIDING CLAMP; BINDING; HYDROLYSIS; PROTEIN; COMPLEX; ROLES; SITES
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/23070
- DOI
- 10.1016/j.bbrc.2007.09.130
- ISSN
- 0006-291X
- Article Type
- Article
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, vol. 364, no. 2, page. 264 - 269, 2007-12-14
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