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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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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2006
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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. |
format | Text |
id | pubmed-1616947 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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