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-Structure paper
Title | MutL binds to 3' resected DNA ends and blocks DNA polymerase access. |
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Journal, issue, pages | Nucleic Acids Res, Vol. 50, Issue 11, Page 6224-6234, Year 2022 |
Publish date | Jun 24, 2022 |
Authors | Alessandro Borsellini / Joyce H G Lebbink / Meindert H Lamers / |
PubMed Abstract | 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 ...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 Å 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. |
External links | Nucleic Acids Res / PubMed:35670670 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.6 Å |
Structure data | EMDB-13255, PDB-7p8v: |
Chemicals | ChemComp-ANP: ChemComp-MG: |
Source |
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Keywords | DNA BINDING PROTEIN / DNA mismatch repair / Protein-DNA complex |