PMID:22001225
| Citation |
Zhang, M, Zhou, Y, Li, T, Wang, H, Cheng, F, Zhou, Y, Bi, L and Zhang, XE (2012) MutL associates with Escherichia coli RecA and inhibits its ATPase activity. Arch. Biochem. Biophys. 517:98-103 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1016/j.abb.2011.09.013 |
| Keywords |
Adenosine Triphosphatases/antagonists & inhibitors; Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; DNA Mismatch Repair; DNA Repair; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; DNA, Single-Stranded/genetics; DNA, Single-Stranded/metabolism; Down-Regulation; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Protein Interaction Domains and Motifs; Rec A Recombinases/antagonists & inhibitors; Rec A Recombinases/chemistry; Rec A Recombinases/metabolism; Recombination, Genetic |
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