Mismatch repair contributes to the overall fidelity of DNA replication by targeting mispaired bases that arise through replication errors during homologous recombination and as a result of DNA damage. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex []. This entry represents a family of evolutionarily related DNA mismatch repair proteins, including MutL, Mlh1, Mlh2 and Mlh3, and Pms 1 and 2. Bacterial MutL proteins are homodimers, while their eukaryotic homologues form heterodimers consisting of the MutL homologue Mlh1 and either Pms1, Pms2 or Mlh3 [, ]. MutL homologues share a conserved ATP binding site [].
This entry represents the N-terminal domain of DNA mismatch repair proteins, such asMutL. Bacterial MutL proteins are homodimers, while their eukaryotic homologues form heterodimers consisting of the MutL homologue Mlh1 and either Pms1, Pms2 or Mlh3 [, ]. MutL proteins and their homologues share sequence homology at their N termini over the first 300-400 residues; the C termini are less well conserved, they constitute the main dimerization domain and are required for interaction between MutL and UvrD helicase []. The activity of the protein is modulated by the ATP-dependent dimerization of the N-terminal domain [].The dimeric MutL protein has a key function in communicating mismatch recognition by MutS to downstream repair processes. Mismatch repair contributes to the overall fidelity of DNA replication by targeting mispaired bases that arise through replication errors during homologous recombination and as a result of DNA damage. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex [].
