ArticleDNA repair2006
Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein.
Article in DNA repair, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
- Molecular dynamics of mismatch detection-How MutS uses indirect readout to find errors in DNA.Biophysical journal · 2023Article
- The properties of Msh2-Msh6 ATP binding mutants suggest a signal amplification mechanism in DNA mismatch repair.The Journal of biological chemistry · 2018Article
- Coordinated protein and DNA conformational changes govern mismatch repair initiation by MutS.Nucleic acids research · 2018Article
- MutSβ abundance and Msh3 ATP hydrolysis activity are important drivers of CTG•CAG repeat expansions.Nucleic acids research · 2017Article
- Evolutionary Covariance Combined with Molecular Dynamics Predicts a Framework for Allostery in the MutS DNA Mismatch Repair Protein.The journal of physical chemistry. B · 2017Article
- Review
- Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair.DNA repair · 2016Review
- Article
- Eukaryotic Mismatch Repair in Relation to DNA Replication.Annual review of genetics · 2015Review
- Slow conformational changes in MutS and DNA direct ordered transitions between mismatch search, recognition and signaling of DNA repair.Journal of molecular biology · 2013Article
- The mechanism of mismatch repair and the functional analysis of mismatch repair defects in Lynch syndrome.Familial cancer · 2013Review
- Structural insights into Saccharomyces cerevisiae Msh4-Msh5 complex function using homology modeling.PloS one · 2013Article
- The hMSH2(M688R) Lynch syndrome mutation may function as a dominant negative.Carcinogenesis · 2012Article
- Large conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.The EMBO journal · 2012Article
- Biochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D).The Journal of biological chemistry · 2012Article
- Mechanism of mismatch recognition revealed by human MutSβ bound to unpaired DNA loops.Nature structural & molecular biology · 2011Article
- Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6.The Journal of biological chemistry · 2011Article
- Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS.Nucleic acids research · 2011Article
- Genetic analysis of baker's yeast Msh4-Msh5 reveals a threshold crossover level for meiotic viability.PLoS genetics · 2010Article
- Magnesium coordination controls the molecular switch function of DNA mismatch repair protein MutS.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Previous analyses of both Thermus aquaticus MutS homodimer and Saccharomyces cerevisiae Msh2-Msh6 heterodimer have revealed that the subunits in these protein complexes bind and hydrolyze ATP asymmetrically, emulating their asymmetric DNA binding properties. In the MutS homodimer, one subunit (S1) binds ATP with high affinity and hydrolyzes it rapidly, while the other subunit (S2) binds ATP with lower affinity and hydrolyzes it at an apparently slower rate. Interaction of MutS with mismatched DNA results in suppression of ATP hydrolysis at S1-but which of these subunits, S1 or S2, makes specific contact with the mismatch (e.g., base stacking by a conserved phenylalanine residue) remains unknown. In order to answer this question and to clarify the links between the DNA binding and ATPase activities of each subunit in the dimer, we made mutations in the ATPase sites of Msh2 and Msh6 and assessed their impact on the activity of the Msh2-Msh6 heterodimer (in Msh2-Msh6, only Msh6 makes base specific contact with the mismatch). The key findings are: (a) Msh6 hydrolyzes ATP rapidly, and thus resembles the S1 subunit of the MutS homodimer, (b) Msh2 hydrolyzes ATP at a slower rate, and thus resembles the S2 subunit of MutS, (c) though itself an apparently weak ATPase, Msh2 has a strong influence on the ATPase activity of Msh6, (d) Msh6 binding to mismatched DNA results in suppression of rapid ATP hydrolysis, revealing a "cis" linkage between its mismatch recognition and ATPase activities, (e) the resultant Msh2-Msh6 complex, with both subunits in the ATP-bound state, exhibits altered interactions with the mismatch.
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