Recombinant Escherichia coli (strain K12) DNA mismatch repair protein MutL

1. In this review, we describe biochemical, biophysical and structural analyses that have clarified how MutL aids at discriminating the newly synthesized strand from its template and marking it for removal. [review] PMID:25701376
2. study found the deletion or insertion of a single LA repeat did not compromise the structural integrity of the protein, nor did it affect MutS- or DNA-binding activity;it severely compromised ATP binding and engagement of the N-terminal domains; both essential activities for proper DNA mismatch repair PMID:23916559
3. MutL accumulates from the mismatch site toward strand discrimination site along the DNA. PMID:22241777
4. Evidence for ATP-dependent structural rearrangement of nuclease catalytic site in DNA mismatch repair endonuclease MutL PMID:21953455
5. C-terminal domain of MutL encompasses a bona fide DNA polymerase III beta-binding motif that mediates a weak, yet specific, interaction between the two proteins. PMID:21050827
6. The presence of phosphate minimizes further MutL oligomerization beyond a dimer PMID:21793594
7. Studies indicate that a stable MutL-ssDNA interaction is unlikely to occur at physiological salt. PMID:21103398
8. MutL homologues play a key role in determining biologic outcome by recruiting and/or activating effector proteins in response to lesion recognition by MutS. PMID:19953589
9. Data report the crystal structure of the Escherichia coli MutL C-terminal dimerization domain and the likelihood of its conservation among MutL homologs. PMID:15470502
10. revised model for the biological dimer, which has important implications for understanding the heterodimerization of eukaryotic MutL homologues, modeling the MutL holoenzyme and predicting protein-protein interaction sites PMID:16024043
11. MutL determines effective DNA homology in recombination processes PMID:17502621
12. An increase in mutL gene copies was also able to partially compensate the hypermutator phenotype of a mutS-defective E. coli derivative. PMID:17825069
13. Results suggest a mobile MutS-MutL complex in DNA mismatch repair signalling, that leaves the DNA mismatch prior to, or at the time of, activation of downstream effector molecules such as Vsr or MutH. PMID:19474347

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KEGG: ecj:JW4128

STRING: 316385.ECDH10B_4365