Nucleic Acids Research Advance Access originally published online on August 25, 2006
Nucleic Acids Research 2006 34(15):4089-4097; doi:10.1093/nar/gkl450
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Nucleic Acids Research, 2006, Vol. 34, No. 15 4089-4097
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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The UvrD helicase and its modulation by the mismatch repair protein MutL
1 Department of Biology, University of North Carolina at Chapel Hill Chapel Hill, NC 27599, USA 2 Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill Chapel Hill, NC 27599, USA 3 Program in Molecular and Cellular Biophysics, University of North Carolina at Chapel Hill Chapel Hill, NC 27599, USA
*To whom correspondence should be addressed. Department of Biology, CB# 3280, Coker Hall, University of North Carolina, Chapel Hill, NC 29577-3280, USA. Tel: +1 919 962 0005; Fax: +1 919 962 1625; Email: smatson{at}bio.unc.edu
Received March 25, 2006. Revised June 11, 2006. Accepted June 14, 2006.
UvrD is a superfamily I DNA helicase with well documented roles in excision repair and methyl-directed mismatch repair (MMR) in addition to poorly understood roles in replication and recombination. The MutL protein is a homodimeric DNA-stimulated ATPase that plays a central role in MMR in Escherichia coli. This protein has been characterized as the master regulator of mismatch repair since it interacts with and modulates the activity of several other proteins involved in the mismatch repair pathway including MutS, MutH and UvrD. Here we present a brief summary of recent studies directed toward arriving at a better understanding of the interaction between MutL and UvrD, and the impact of this interaction on the activity of UvrD and its role in mismatch repair.
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