The mismatch repair factor Mlh1-Pms1 uses ATP to compact and remodel DNA.

ABSTRACT: In eukaryotes, mismatch repair begins with MutS homolog (MSH) complexes, which scan newly replicated DNA for mismatches. Upon mismatch detection, MSH complexes recruit the PCNA-stimulated endonuclease Mlh1-Pms1/PMS2 (yeast/human), which nicks the DNA to allow downstream proteins to remove the mismatch. Past work has shown that although Mlh1-Pms1 is an ATPase and this activity is important in vivo, ATP is not required to nick DNA. Our data, using yeast as a model, suggests that Mlh1-Pms1 forms oligomeric complexes that drive DNA conformational rearrangements using the protein's ATPase activity. Experiments with non-B-form DNA structures, common in microsatellite regions, show that these structures inhibit Mlh1-Pms1's activities, likely through impeding Mlh1-Pms1-dependent DNA conform

SUBMITTER: Collingwood BW 

PROVIDER: S-EPMC11760735 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature