期刊
MOLECULAR CELL
卷 26, 期 4, 页码 565-578出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.04.024
关键词
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资金
- NCI NIH HHS [CA92584, P01 CA092584, P01 CA092584-06] Funding Source: Medline
- NIGMS NIH HHS [R01 GM050006-19, T32 GM008666, R01 GM050006, T32 GM08666, GM50006] Funding Source: Medline
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.
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