PMID:22001225

Citation	Zhang, M, Zhou, Y, Li, T, Wang, H, Cheng, F, Zhou, Y, Bi, L and Zhang, XE (2011) MutL associates with Escherichia coli RecA and inhibits its ATPase activity.Arch Biochem Biophys
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
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Phenotype of	Taxon Information	Genotype Information (if known)	Condition Information	OMP ID	OMP Term Name	ECO ID	ECO Term Name	Notes	Status
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Notes

Purified MutL binds to purified RecA and inhibits RecA's ssDNA-dependent ATPase activity without affecting the interaction of RecA and single-stranded DNA. An ATPase deficient MutL mutant (E29A) has the same effect on RecA as wild-type MutL. The N-terminal fragment of MutL (amino acid residues 1-349) can bind to RecA, but its effect on the ATPase activity of RecA wasn't tested.

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