Structural highlights
Function
[MUTL_ECOLI] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA.
Publication Abstract from PubMed
DNA mismatch repair removes mis-incorporated bases after DNA replication and reduces the error rate a 100-1000-fold. After recognition of a mismatch, a large section of up to a thousand nucleotides is removed from the daughter strand followed by re-synthesis. How these opposite activities are coordinated is poorly understood. Here we show that the Escherichia coli MutL protein binds to the 3' end of the resected strand and blocks access of Pol I and Pol III. The cryo-EM structure of an 85-kDa MutL-DNA complex, determined to 3.7 A resolution, reveals a unique DNA binding mode that positions MutL at the 3' end of a primer-template, but not at a 5' resected DNA end or a blunt DNA end. Hence, our work reveals a novel role for MutL in the final stages of mismatch repair by preventing premature DNA synthesis during removal of the mismatched strand.
MutL binds to 3' resected DNA ends and blocks DNA polymerase access.,Borsellini A, Lebbink JHG, Lamers MH Nucleic Acids Res. 2022 Jun 24;50(11):6224-6234. doi: 10.1093/nar/gkac432. PMID:35670670[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Borsellini A, Lebbink JHG, Lamers MH. MutL binds to 3' resected DNA ends and blocks DNA polymerase access. Nucleic Acids Res. 2022 Jun 24;50(11):6224-6234. doi: 10.1093/nar/gkac432. PMID:35670670 doi:http://dx.doi.org/10.1093/nar/gkac432
