Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair
about
hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication fociCadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complexThe alternating ATPase domains of MutS control DNA mismatch repairCrystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repairPostreplicative mismatch repair.Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha.Saccharomyces cerevisiae Mer3 is a DNA helicase involved in meiotic crossing overA mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition.exo1-Dependent mutator mutations: model system for studying functional interactions in mismatch repair.Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination.Analysis of the functional domains of the mismatch repair homologue Msh1p and its role in mitochondrial genome maintenance.DNA mismatch repair and mutation avoidance pathwaysLarge conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.Msh2 ATPase activity is essential for somatic hypermutation at a-T basepairs and for efficient class switch recombinationDNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiaeMsh2 blocks an alternative mechanism for non-homologous tail removal during single-strand annealing in Saccharomyces cerevisiaeSaccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair.Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.Isolation and characterization of point mutations in mismatch repair genes that destabilize microsatellites in yeast.Distinct roles for the Saccharomyces cerevisiae mismatch repair proteins in heteroduplex rejection, mismatch repair and nonhomologous tail removalDynamical allosterism in the mechanism of action of DNA mismatch repair protein MutS.Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS.The predicted truncation from a cancer-associated variant of the MSH2 initiation codon alters activity of the MSH2-MSH6 mismatch repair complexMutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function.Functional characterization of pathogenic human MSH2 missense mutations in Saccharomyces cerevisiae.Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein.Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.A Delicate Balance Between Repair and Replication Factors Regulates Recombination Between Divergent DNA Sequences in Saccharomyces cerevisiaeCoDP: predicting the impact of unclassified genetic variants in MSH6 by the combination of different properties of the protein.Evidence that msh1p plays multiple roles in mitochondrial base excision repair.Multiple factors insulate Msh2-Msh6 mismatch repair activity from defects in Msh2 domain I.Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP.Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6.Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair.Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA.Mph1 requires mismatch repair-independent and -dependent functions of MutSalpha to regulate crossover formation during homologous recombination repair.Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair.Novel dominant mutations in Saccharomyces cerevisiae MSH6.The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair.Distinct nucleotide binding/hydrolysis properties and molar ratio of MutSalpha and MutSbeta determine their differential mismatch binding activities.
P2860
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P2860
Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Saccharomyces cerevisiae Msh2p ...... equired during mismatch repair
@ast
Saccharomyces cerevisiae Msh2p ...... equired during mismatch repair
@en
Saccharomyces cerevisiae Msh2p ...... quired during mismatch repair.
@nl
type
label
Saccharomyces cerevisiae Msh2p ...... equired during mismatch repair
@ast
Saccharomyces cerevisiae Msh2p ...... equired during mismatch repair
@en
Saccharomyces cerevisiae Msh2p ...... quired during mismatch repair.
@nl
prefLabel
Saccharomyces cerevisiae Msh2p ...... equired during mismatch repair
@ast
Saccharomyces cerevisiae Msh2p ...... equired during mismatch repair
@en
Saccharomyces cerevisiae Msh2p ...... quired during mismatch repair.
@nl
P2093
P2860
P356
P1476
Saccharomyces cerevisiae Msh2p ...... equired during mismatch repair
@en
P2093
P2860
P304
P356
10.1128/MCB.18.12.7590
P407
P577
1998-12-01T00:00:00Z