Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition.
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Interactions of human hMSH2 with hMSH3 and hMSH2 with hMSH6: examination of mutations found in hereditary nonpolyposis colorectal cancer.hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA.Mechanism of mismatch recognition revealed by human MutSĪ² bound to unpaired DNA loopsN-terminus of hMLH1 confers interaction of hMutLalpha and hMutLbeta with hMutSalphaPostreplicative mismatch repair.Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha.Conserved properties between functionally distinct MutS homologs in yeastSaccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repairA mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition.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.Caenorhabditis elegans msh-5 is required for both normal and radiation-induced meiotic crossing over but not for completion of meiosisDNA mismatch repair and mutation avoidance pathwaysNucleotides and heteroduplex DNA preserve the active conformation of Pseudomonas aeruginosa MutS by preventing protein oligomerizationThe role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switchNucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanismMsh2 blocks an alternative mechanism for non-homologous tail removal during single-strand annealing in Saccharomyces cerevisiaeMSH2 ATPase domain mutation affects CTG*CAG repeat instability in transgenic mice.Genetic analysis of baker's yeast Msh4-Msh5 reveals a threshold crossover level for meiotic viability.Crossing over during Caenorhabditis elegans meiosis requires a conserved MutS-based pathway that is partially dispensable in budding yeastInteractions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.Caenorhabditis elegans DNA mismatch repair gene msh-2 is required for microsatellite stability and maintenance of genome integrity.Functional overlap in mismatch repair by human MSH3 and MSH6.EXO1 and MSH6 are high-copy suppressors of conditional mutations in the MSH2 mismatch repair gene of Saccharomyces cerevisiae.Mutator phenotypes of yeast strains heterozygous for mutations in the MSH2 gene.Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6Meiotic recombination intermediates and mismatch repair proteins.Single-molecule motions and interactions in live cells reveal target search dynamics in mismatch repair.Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.The hMSH2(M688R) Lynch syndrome mutation may function as a dominant negative.Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations.Hereditary cancer-associated missense mutations in hMSH6 uncouple ATP hydrolysis from DNA mismatch binding.Evidence that msh1p plays multiple roles in mitochondrial base excision repair.Reciprocal regulation of nuclear import of the yeast MutSalpha DNA mismatch repair proteins Msh2 and Msh6.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.ATP-hydrolysis-dependent conformational switch modulates the stability of MutS-mismatch complexes.Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA.DNA-dependent activation of the hMutSalpha ATPase.hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha
P2860
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P2860
Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition.
description
1997 nĆ® lÅ«n-bĆ»n
@nan
1997 Õ©ÕøÖÕ”ÕÆÕ”Õ¶Õ« ÕÕ”ÕµÕ«Õ½Õ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕøÖÕ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ ÕµÖ
Õ¤ÕøÖÕ”Õ®
@hyw
1997 Õ©Õ¾Õ”ÕÆÕ”Õ¶Õ« Õ“Õ”ÕµÕ«Õ½Õ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕ¾Õ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ Õ°ÕøÕ¤Õ¾Õ”Õ®
@hy
1997幓ć®č«ę
@ja
1997幓č«ę
@yue
1997幓č«ę
@zh-hant
1997幓č«ę
@zh-hk
1997幓č«ę
@zh-mo
1997幓č«ę
@zh-tw
1997幓č®ŗę
@wuu
name
Genetic and biochemical analys ...... ismatch base pair recognition.
@ast
Genetic and biochemical analys ...... ismatch base pair recognition.
@en
Genetic and biochemical analys ...... ismatch base pair recognition.
@nl
type
label
Genetic and biochemical analys ...... ismatch base pair recognition.
@ast
Genetic and biochemical analys ...... ismatch base pair recognition.
@en
Genetic and biochemical analys ...... ismatch base pair recognition.
@nl
prefLabel
Genetic and biochemical analys ...... ismatch base pair recognition.
@ast
Genetic and biochemical analys ...... ismatch base pair recognition.
@en
Genetic and biochemical analys ...... ismatch base pair recognition.
@nl
P2093
P2860
P356
P1476
Genetic and biochemical analys ...... mismatch base pair recognition
@en
P2093
P2860
P304
P356
10.1128/MCB.17.5.2436
P407
P50
P577
1997-05-01T00:00:00Z