Identification of Exo1-Msh2 interaction motifs in DNA mismatch repair and new Msh2-binding partners

@article{Goellner2018IdentificationOE,
  title={Identification of Exo1-Msh2 interaction motifs in DNA mismatch repair and new Msh2-binding partners},
  author={Eva M. Goellner and C. Putnam and W. J. Graham and Christine M Rahal and Bin-zhong Li and R. Kolodner},
  journal={Nature Structural \& Molecular Biology},
  year={2018},
  volume={25},
  pages={650-659}
}
Eukaryotic DNA mismatch repair (MMR) involves both exonuclease 1 (Exo1)-dependent and Exo1-independent pathways. We found that the unstructured C-terminal domain of Saccharomyces cerevisiae Exo1 contains two MutS homolog 2 (Msh2)-interacting peptide (SHIP) boxes downstream from the MutL homolog 1 (Mlh1)-interacting peptide (MIP) box. These three sites were redundant in Exo1-dependent MMR in vivo and could be replaced by a fusion protein between an N-terminal fragment of Exo1 and Msh6. The SHIP… Expand
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