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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-08

AUTHORS

Eva M. Goellner, Christopher D. Putnam, William J. Graham, Christine M. Rahal, Bin-Zhong Li, Richard D. Kolodner

ABSTRACT

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-Msh2 interactions were eliminated by the msh2M470I mutation, and wild-type but not mutant SHIP peptides eliminated Exo1-dependent MMR in vitro. We identified two S. cerevisiae SHIP-box-containing proteins and three candidate human SHIP-box-containing proteins. One of these, Fun30, had a small role in Exo1-dependent MMR in vivo. The Remodeling of the Structure of Chromatin (Rsc) complex also functioned in both Exo1-dependent and Exo1-independent MMR in vivo. Our results identified two modes of Exo1 recruitment and a peptide module that mediates interactions between Msh2 and other proteins, and they support a model in which Exo1 functions in MMR by being tethered to the Msh2-Msh6 complex. More... »

PAGES

650-659

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41594-018-0092-y

DOI

http://dx.doi.org/10.1038/s41594-018-0092-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1105832127

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30061603


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