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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 Escherichi...

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Detalles Bibliográficos
Autores principales: Matson, Steven W., Robertson, Adam B.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616947/
https://www.ncbi.nlm.nih.gov/pubmed/16935885
http://dx.doi.org/10.1093/nar/gkl450
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author Matson, Steven W.
Robertson, Adam B.
author_facet Matson, Steven W.
Robertson, Adam B.
author_sort Matson, Steven W.
collection PubMed
description 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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spelling pubmed-16169472006-10-27 The UvrD helicase and its modulation by the mismatch repair protein MutL Matson, Steven W. Robertson, Adam B. Nucleic Acids Res Survey and Summary 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. Oxford University Press 2006-09 2006-08-25 /pmc/articles/PMC1616947/ /pubmed/16935885 http://dx.doi.org/10.1093/nar/gkl450 Text en © 2006 The Author(s)
spellingShingle Survey and Summary
Matson, Steven W.
Robertson, Adam B.
The UvrD helicase and its modulation by the mismatch repair protein MutL
title The UvrD helicase and its modulation by the mismatch repair protein MutL
title_full The UvrD helicase and its modulation by the mismatch repair protein MutL
title_fullStr The UvrD helicase and its modulation by the mismatch repair protein MutL
title_full_unstemmed The UvrD helicase and its modulation by the mismatch repair protein MutL
title_short The UvrD helicase and its modulation by the mismatch repair protein MutL
title_sort uvrd helicase and its modulation by the mismatch repair protein mutl
topic Survey and Summary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616947/
https://www.ncbi.nlm.nih.gov/pubmed/16935885
http://dx.doi.org/10.1093/nar/gkl450
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