ArticleNucleic acids research2007
Multiple functions for the N-terminal region of Msh6.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- An integrative pan-cancer analysis reveals the oncogenic role of mutS homolog 6 (MSH6) in human tumors.Aging · 2021Article
- Mismatch repair single nucleotide polymorphisms and thyroid cancer susceptibility.Oncology letters · 2018Article
- Article
- Review
- Multiple factors insulate Msh2-Msh6 mismatch repair activity from defects in Msh2 domain I.Journal of molecular biology · 2011Article
- Cooperative nuclear localization sequences lend a novel role to the N-terminal region of MSH6.PloS one · 2011Article
- Phosphorylated hMSH6: DNA mismatch versus DNA damage recognition.Mutation research · 2011Article
- Msh6 protects mature B cells from lymphoma by preserving genomic stability.The American journal of pathology · 2010Article
- MSH2/MSH6 complex promotes error-free repair of AID-induced dU:G mispairs as well as error-prone hypermutation of A:T sites.PloS one · 2010Article
- MSH6 mutations arise in glioblastomas during temozolomide therapy and mediate temozolomide resistance.Clinical cancer research : an official journal of the American Association for Cancer Research · 2009Article
- Regulation of interactions with sliding clamps during DNA replication and repair.Current genomics · 2009Article
- Article
- Structural, molecular and cellular functions of MSH2 and MSH6 during DNA mismatch repair, damage signaling and other noncanonical activities.Mutation researchReview
- DNA mismatch repair: molecular mechanism, cancer, and ageing.Mechanisms of ageing and developmentReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The eukaryotic mismatch repair protein Msh6 shares five domains in common with other MutS members. However, it also contains several hundred additional residues at its N-terminus. A few of these residues bind to PCNA, but the functions of the other amino acids in the N-terminal region (NTR) are unknown. Here we demonstrate that the Msh6 NTR binds to duplex DNA in a salt-sensitive, mismatch-independent manner. Partial proteolysis, DNA affinity chromatography and mass spectrometry identified a fragment comprised of residues 228-299 of yeast Msh6 that binds to DNA and is rich in positively charged residues. Deleting these residues, or replacing lysines and arginines with glutamate, reduces DNA binding in vitro and elevates spontaneous mutation rates and resistance to MNNG treatment in vivo. Similar in vivo defects are conferred by alanine substitutions in a highly conserved motif in the NTR that immediately precedes domain I of MutS proteins, the domain that interacts with mismatched DNA. These data suggest that, in addition to PCNA binding, DNA binding and possibly other functions in the amino terminal region of Msh6 are important for eukaryotic DNA mismatch repair and cellular response to alkylation damage.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.