The UvrD helicase and its modulation by the mismatch repair protein MutL.
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.
Matson
Steven W
SW
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. smatson@bio.unc.edu
Robertson
Adam B
AB
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D020137:Base Pair Mismatch; D004265:DNA Helicases / Q000378:metabolism*; D004260:DNA Repair / Q000502:physiology*; D004261:DNA Replication / Q000502:physiology; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D000070956:MutL Proteins
D029968:Escherichia coli Proteins; C074770:MutL protein, E coli; D000251:Adenosine Triphosphatases; C506746:UvrD protein, E coli; D000070956:MutL Proteins; D004265:DNA Helicases