ArticleThe EMBO journal2011
Atomic force microscopy captures MutS tetramers initiating DNA mismatch repair.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- A high-throughput single-molecule platform to study DNA supercoiling effect on protein-DNA interactions.Nucleic acids research · 2025Article
- Atomic Force Microscopy Reveals that the Drosophila Telomere-Capping Protein Verrocchio Is a Single-Stranded DNA-Binding Protein.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Dynamic human MutSα-MutLα complexes compact mismatched DNA.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Molecular Spectroscopic Markers of DNA Damage.Molecules (Basel, Switzerland) · 2020Review
- The unstructured linker arms of MutL enable GATC site incision beyond roadblocks during initiation of DNA mismatch repair.Nucleic acids research · 2019Article
- Single gold-bridged nanoprobes for identification of single point DNA mutations.Nature communications · 2019Article
- 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
- Visualizing correlated motion with HDBSCAN clustering.Protein science : a publication of the Protein Society · 2018Article
- A 'Semi-Protected Oligonucleotide Recombination' Assay for DNA Mismatch Repair in vivo Suggests Different Modes of Repair for Lagging Strand Mismatches.Nucleic acids research · 2017Article
- MutSFrontiers in physics · 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
- Visualizing the Path of DNA through Proteins Using DREEM Imaging.Molecular cell · 2016Article
- Atomic force microscopy captures the initiation of methyl-directed DNA mismatch repair.DNA repair · 2015Article
- Probing fibronectin-antibody interactions using AFM force spectroscopy and lateral force microscopy.Beilstein journal of nanotechnology · 2015Article
- Free-energy calculations for semi-flexible macromolecules: applications to DNA knotting and looping.The Journal of chemical physics · 2014Article
- Single molecule studies of DNA mismatch repair.DNA repair · 2014Review
- Probing transient protein-mediated DNA linkages using nanoconfinement.Biomicrofluidics · 2014Article
- Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation.Nucleic acids research · 2013Article
- Mismatch repair inhibits homeologous recombination via coordinated directional unwinding of trapped DNA structures.Molecular cell · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 3 countries.
Funding
Abstract
In spite of extensive research, the mechanism by which MutS initiates DNA mismatch repair (MMR) remains controversial. We use atomic force microscopy (AFM) to capture how MutS orchestrates the first step of E. coli MMR. AFM images captured two types of MutS/DNA complexes: single-site binding and loop binding. In most of the DNA loops imaged, two closely associated MutS dimers formed a tetrameric complex in which one of the MutS dimers was located at or near the mismatch. Surprisingly, in the presence of ATP, one MutS dimer remained at or near the mismatch site and the other, while maintaining contact with the first dimer, relocated on the DNA by reeling in DNA, thereby producing expanding DNA loops. Our results indicate that MutS tetramers composed of two non-equivalent MutS dimers drive E. coli MMR, and these new observations now reconcile the apparent contradictions of previous 'sliding' and 'bending/looping' models of interaction between mismatch and strand signal.
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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.