ArticleNucleic acids research2012
Single-molecule multiparameter fluorescence spectroscopy reveals directional MutS binding to mismatched bases in DNA.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- A robust luminescent assay for screening alkyladenine DNA glycosylase inhibitors to overcome DNA repair and temozolomide drug resistance.Journal of pharmaceutical analysis · 2023Article
- Unraveling the hidden temporal range of fast βCommunications biology · 2022Article
- Multi-parameter photon-by-photon hidden Markov modeling.Nature communications · 2022Article
- Cryogenic electron microscopy structures reveal how ATP and DNA binding in MutS coordinates sequential steps of DNA mismatch repair.Nature structural & molecular biology · 2022Article
- Probing DNA-protein interactions using single-molecule diffusivity contrast.Biophysical reports · 2021Article
- DNA sequence-dependent positioning of the linker histone in a nucleosome: A single-pair FRET study.Biophysical journal · 2021Article
- ABEL-FRET: tether-free single-molecule FRET with hydrodynamic profiling.Nature methods · 2021Article
- Substrate conformational dynamics facilitate structure-specific recognition of gapped DNA by DNA polymerase.Nucleic acids research · 2019Article
- Mismatch Recognition byInternational journal of molecular sciences · 2019Article
- MutSγ-Induced DNA Conformational Changes Provide Insights into Its Role in Meiotic Recombination.Biophysical journal · 2018Article
- Coordinated protein and DNA conformational changes govern mismatch repair initiation by MutS.Nucleic acids research · 2018Article
- High precision FRET studies reveal reversible transitions in nucleosomes between microseconds and minutes.Nature communications · 2018Article
- Combining Graphical and Analytical Methods with Molecular Simulations To Analyze Time-Resolved FRET Measurements of Labeled Macromolecules Accurately.The journal of physical chemistry. B · 2017Article
- Using Atomic Force Microscopy to Characterize the Conformational Properties of Proteins and Protein-DNA Complexes That Carry Out DNA Repair.Methods in enzymology · 2017Article
- Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair.DNA repair · 2016Review
- Atomic force microscopy captures the initiation of methyl-directed DNA mismatch repair.DNA repair · 2015Article
- Article
- Dye label interference with RNA modification reveals 5-fluorouridine as non-covalent inhibitor.Nucleic acids research · 2014Article
- Single molecule studies of DNA mismatch repair.DNA repair · 2014Review
- Dynamics of MutS-mismatched DNA complexes are predictive of their repair phenotypes.Biochemistry · 2014Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mismatch repair (MMR) corrects replication errors such as mismatched bases and loops in DNA. The evolutionarily conserved dimeric MMR protein MutS recognizes mismatches by stacking a phenylalanine of one subunit against one base of the mismatched pair. In all crystal structures of G:T mismatch-bound MutS, phenylalanine is stacked against thymine. To explore whether these structures reflect directional mismatch recognition by MutS, we monitored the orientation of Escherichia coli MutS binding to mismatches by FRET and anisotropy with steady state, pre-steady state and single-molecule multiparameter fluorescence measurements in a solution. The results confirm that specifically bound MutS bends DNA at the mismatch. We found additional MutS-mismatch complexes with distinct conformations that may have functional relevance in MMR. The analysis of individual binding events reveal significant bias in MutS orientation on asymmetric mismatches (G:T versus T:G, A:C versus C:A), but not on symmetric mismatches (G:G). When MutS is blocked from binding a mismatch in the preferred orientation by positioning asymmetric mismatches near the ends of linear DNA substrates, its ability to authorize subsequent steps of MMR, such as MutH endonuclease activation, is almost abolished. These findings shed light on prerequisites for MutS interactions with other MMR proteins for repairing the appropriate DNA strand.
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