Abstract
Different DNA repair systems are known to cooperate to deal with DNA damage. However, the regulatory role of the cross-talk between these pathways is unclear. Here, we have shown that MutL, an essential component of mismatch repair, is a RecA-interacting protein, and that its highly conserved N-terminal domain is sufficient for this interaction. Surface plasmon resonance and capillary electrophoresis analyses revealed that MutL has little effect on RecA-ssDNA filament formation, but dose down-regulate the ATPase activity of RecA. Our findings identify a new role for MutL, and suggest its regulatory role in homologous recombination.
Copyright © 2011. Published by Elsevier Inc.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / antagonists & inhibitors
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / metabolism*
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DNA Mismatch Repair
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DNA Repair
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DNA, Bacterial / genetics
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DNA, Bacterial / metabolism
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DNA, Single-Stranded / genetics
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DNA, Single-Stranded / metabolism
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Down-Regulation
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / metabolism*
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MutL Proteins
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Protein Interaction Domains and Motifs
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Rec A Recombinases / antagonists & inhibitors
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Rec A Recombinases / chemistry
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Rec A Recombinases / metabolism*
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Recombination, Genetic
Substances
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DNA, Bacterial
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DNA, Single-Stranded
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Escherichia coli Proteins
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MutL protein, E coli
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Rec A Recombinases
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Adenosine Triphosphatases
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MutL Proteins