Effect of E. coli MutL on the steady-state ATPase activity of MutS in the presence of short blocked end DNAs
SCIE
SCOPUS
- Title
- Effect of E. coli MutL on the steady-state ATPase activity of MutS in the presence of short blocked end DNAs
- Authors
- Heo, SD; Ku, JK; Ban, C
- Date Issued
- 2009-07-24
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Abstract
- The effect of wild-type and mutant MULL on the steady-state ATPase activity of MutS from Escherichia coli has been investigated in the absence and presence of 22, 50, and 75 base pair hetero- and homoduplex DNAs with open and blocked ends. The steady-state ATPase activity of MutS has been measured at 37 degrees C using a spectrophotometric method. The presence Of MutL did not affect appreciably on the ATPase activity of MutS in the absence of DNA or in the presence of blocked end homoduplex DNAs. However, the addition of MULL affected oppositely on the ATPase activity of MutS in the presence of G-T mismatched DNAs depending on their end status. We have also found that only the ATPase active forms of MutL increased the ATPase activity of MutS in the presence of G-T mismatched DNAs with blocked ends. The results suggest that MutL ATPase activity is required to catalyze dissociation of the MutS sliding clamps. (C) 2009 Elsevier Inc. All rights reserved.
- Keywords
- MutL; MutS; MMR mechanism; ATPase activity; Blocked heteroduplex DNA; MISMATCH REPAIR; HYDROLYSIS; MODULATION; DOMAINS; BINDING; SWITCH
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/27869
- DOI
- 10.1016/j.bbrc.2009.05.042
- ISSN
- 0006-291X
- Article Type
- Article
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, vol. 385, no. 2, page. 225 - 229, 2009-07-24
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.