Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex (Q28142999)

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scientific article (publication date: November 2000)

Language	Label	Description	Also known as
English	Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex	scientific article (publication date: November 2000)

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scholarly article

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Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex (English)

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author name string

H Flores-Rozas

1

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D Clark

2

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R D Kolodner

3

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language of work or name

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publication date

November 2000

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Nature Genetics

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26

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3

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375-8

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ATP-dependent interaction of human mismatch repair proteins and dual role of PCNA in mismatch repair

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Evidence for involvement of yeast proliferating cell nuclear antigen in DNA mismatch repair

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Requirement for PCNA in DNA mismatch repair at a step preceding DNA resynthesis

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Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts

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DNA-replication fidelity, mismatch repair and genome instability in cancer cells

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PCNA binding through a conserved motif

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Saccharomyces cerevisiae pol30 (proliferating cell nuclear antigen) mutations impair replication fidelity and mismatch repair

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A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair

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Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA.

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The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch

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Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition.

1 reference

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Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism

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hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha

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Eukaryotic DNA mismatch repair

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MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast

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Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex

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The Escherichia coli MutL protein stimulates binding of Vsr and MutS to heteroduplex DNA.

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The MutL ATPase is required for mismatch repair

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The distribution of the numbers of mutants in bacterial populations

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The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations

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Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair

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The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs

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Identification of replication factor C from Saccharomyces cerevisiae: a component of the leading-strand DNA replication complex

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Microsatellite instability in yeast: dependence on repeat unit size and DNA mismatch repair genes

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