ArticleThe Journal of biological chemistry2011
Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Mismatch Repair Protein Msh6International journal of molecular sciences · 2023Article
- Expression differences between proteins responsible for DNA damage repair according to the Gleason grade as a new heterogeneity marker in prostate cancer.Archives of medical science : AMS · 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
- Coordinating Multi-Protein Mismatch Repair by Managing Diffusion Mechanics on the DNA.Journal of molecular biology · 2018Review
- MutS homolog sliding clamps shield the DNA from binding proteins.The Journal of biological chemistry · 2018Article
- 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
- Cascading MutS and MutL sliding clamps control DNA diffusion to activate mismatch repair.Nature · 2016Article
- Dynamic control of strand excision during human DNA mismatch repair.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function.BMC microbiology · 2016Article
- Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair.DNA repair · 2016Review
- Mismatch repair.The Journal of biological chemistry · 2015Review
- Mismatch repair during homologous and homeologous recombination.Cold Spring Harbor perspectives in biology · 2015Review
- Single-molecule views of MutS on mismatched DNA.DNA repair · 2014Review
- Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break 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
- Postreplicative mismatch repair.Cold Spring Harbor perspectives in biology · 2013Review
- Defining the nature of human γδ T cells: a biographical sketch of the highly empathetic.Cellular & molecular immunology · 2013Review
- Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
The mechanics of hMSH2-hMSH6 ATP binding and hydrolysis are critical to several proposed mechanisms for mismatch repair (MMR), which in turn rely on the detailed coordination of ATP processing between the individual hMSH2 and hMSH6 subunits. Here we show that hMSH2-hMSH6 is strictly controlled by hMSH2 and magnesium in a complex with ADP (hMSH2(magnesium-ADP)-hMSH6). Destabilization of magnesium results in ADP release from hMSH2 that allows high affinity ATP binding by hMSH6, which then enhances ATP binding by hMSH2. Both subunits must be ATP-bound to efficiently form a stable hMSH2-hMSH6 hydrolysis-independent sliding clamp required for MMR. In the presence of magnesium, the ATP-bound sliding clamps remain on the DNA for ∼8 min. These results suggest a precise stepwise kinetic mechanism for hMSH2-hMSH6 functions that appears to mimic G protein switches, severely constrains models for MMR, and may partially explain the MSH2 allele frequency in Lynch syndrome or hereditary nonpolyposis colorectal cancer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.