ArticleThe Journal of biological chemistry2010
Magnesium coordination controls the molecular switch function of DNA mismatch repair protein MutS.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 56 citations in OpenAlex.
- Article
- Article
- Backbone Conformational Equilibrium in Mismatched DNA Correlates with Enzyme Activity.Biochemistry · 2023Article
- Molecular dynamics of mismatch detection-How MutS uses indirect readout to find errors in DNA.Biophysical journal · 2023Article
- Importance of base-pair opening for mismatch recognition.Nucleic acids research · 2020Article
- Comprehensive classification of ABC ATPases and their functional radiation in nucleoprotein dynamics and biological conflict systems.Nucleic acids research · 2020Review
- Recurrent mismatch binding by MutS mobile clamps on DNA localizes repair complexes nearby.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The unstructured linker arms of MutL enable GATC site incision beyond roadblocks during initiation of DNA mismatch repair.Nucleic acids research · 2019Article
- Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage.Nucleic acids research · 2019Article
- Sharp kinking of a coiled-coil in MutS allows DNA binding and release.Nucleic acids research · 2019Article
- Bending of DNA duplexes with mutation motifs.DNA research : an international journal for rapid publication of reports on genes and genomes · 2019Article
- Molecular switch-like regulation enables global subunit coordination in a viral ring ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Berkeley Screen: a set of 96 solutions for general macromolecular crystallization.Journal of applied crystallography · 2017Article
- Dual daughter strand incision is processive and increases the efficiency of DNA mismatch repair.Nucleic acids research · 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
- Article
- The structural impact of DNA mismatches.Nucleic acids research · 2015Article
- Real-time surface plasmon resonance study of biomolecular interactions between polymerase and bulky mutagenic DNA lesions.Chemical research in toxicology · 2014Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DNA mismatch repair protein MutS acts as a molecular switch. It toggles between ADP and ATP states and is regulated by mismatched DNA. This is analogous to G-protein switches and the regulation of their "on" and "off" states by guanine exchange factors. Although GDP release in monomeric GTPases is accelerated by guanine exchange factor-induced removal of magnesium from the catalytic site, we found that release of ADP from MutS is not influenced by the metal ion in this manner. Rather, ADP release is induced by the binding of mismatched DNA at the opposite end of the protein, a long-range allosteric response resembling the mechanism of activation of heterotrimeric GTPases. Magnesium influences switching in MutS by inducing faster and tighter ATP binding, allowing rapid downstream responses. MutS mutants with decreased affinity for the metal ion are impaired in fast switching and in vivo mismatch repair. Thus, the G-proteins and MutS conceptually employ the same efficient use of the high energy cofactor: slow hydrolysis in the absence of a signal and fast conversion to the active state when required.
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