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• W2113548088 abstract "The eukaryotic MutS homolog complexes, Msh2-Msh6 and Msh2-Msh3, recognize mismatched bases in DNA during mismatch repair (MMR). The eukaryote-specific N-terminal regions (NTRs) of Msh6 and Msh3 have not been characterized other than by demonstrating that they contain an N-terminal PCNA-interacting motif. Here we have demonstrated genetically that the NTR of Msh6 has an important role in MMR that is partially redundant with PCNA binding. Small-angle X-ray scattering (SAXS) was used to determine the solution structure of the complex of PCNA with Msh2-Msh6 and with the isolated Msh6 NTR, revealing that the Msh6 NTR is a natively disordered domain that forms an extended tether between Msh6 and PCNA. Moreover, computational analysis of PCNA-interacting motifs in the S. cerevisiae proteome indicated that flexible linkers are a common theme for PCNA-interacting proteins that may serve to localize these binding partners without tightly restraining them to the immediate vicinity of PCNA." @default.
• W2113548088 created "2016-06-24" @default.
• W2113548088 creator A5028696052 @default.
• W2113548088 creator A5081915207 @default.
• W2113548088 creator A5083302085 @default.
• W2113548088 date "2007-05-01" @default.
• W2113548088 modified "2023-10-13" @default.
• W2113548088 title "The N Terminus of Saccharomyces cerevisiae Msh6 Is an Unstructured Tether to PCNA" @default.
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• W2113548088 doi "https://doi.org/10.1016/j.molcel.2007.04.024" @default.
• W2113548088 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2001284" @default.
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• W2113548088 hasPublicationYear "2007" @default.
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