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 |
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| 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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Main Points of the Paper
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Materials and Methods Used
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Phenotype Annotations
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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.
References
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