ArticleProceedings of the National Academy of Sciences of the United States of America2012
Single-molecule imaging of DNA curtains reveals mechanisms of KOPS sequence targeting by the DNA translocase FtsK.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- A novel high-throughput single-molecule technique DNA curtain: Applications for DNA metabolism.Molecules and cells · 2025Review
- Single-molecule DNA-flow stretching assay as a versatile hybrid tool for investigating DNA-protein interactions.BMB reports · 2025Review
- Proteomic Profiling inACS omega · 2024Article
- Molecular dynamics of DNA translocation by FtsK.Nucleic acids research · 2022Article
- Single-molecule fluorescence imaging techniques reveal molecular mechanisms underlying deoxyribonucleic acid damage repair.Frontiers in bioengineering and biotechnology · 2022Review
- Studying R-Loop Recognizing Proteins Using Single-Molecule DNA Curtain Technique and Electrophoretic Mobility Shift Assay.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Single-Molecule Imaging Reveals the Mechanism Underlying Histone Loading ofMolecules and cells · 2021Article
- FtsK in motion reveals its mechanism for double-stranded DNA translocation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Single-molecule visualization reveals the damage search mechanism for the human NER protein XPC-RAD23B.Nucleic acids research · 2019Article
- The FtsK-like motor TraB is a DNA-dependent ATPase that forms higher-order assemblies.The Journal of biological chemistry · 2019Article
- DNA scanning by base excision repair enzymes and implications for pathway coordination.DNA repair · 2018Review
- Facilitated Unbinding via Multivalency-Enabled Ternary Complexes: New Paradigm for Protein-DNA Interactions.Accounts of chemical research · 2018Review
- Mechanochemical coupling and bi-phasic force-velocity dependence in the ultra-fast ring ATPase SpoIIIE.eLife · 2018Article
- High Free-Energy Barrier of 1D Diffusion Along DNA by Architectural DNA-Binding Proteins.Journal of molecular biology · 2018Article
- Kinetics of large-scale chromosomal movement during asymmetric cell division in Escherichia coli.PLoS genetics · 2017Article
- Xer Site Specific Recombination: Double and Single Recombinase Systems.Frontiers in microbiology · 2017Review
- Biological Nanomotors with a Revolution, Linear, or Rotation Motion Mechanism.Microbiology and molecular biology reviews : MMBR · 2016Review
- Single-molecule imaging reveals the mechanism of Exo1 regulation by single-stranded DNA binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Two-subunit DNA escort mechanism and inactive subunit bypass in an ultra-fast ring ATPase.eLife · 2015Article
- Assembly, translocation, and activation of XerCD-dif recombination by FtsK translocase analyzed in real-time by FRET and two-color tethered fluorophore motion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
5 authors.
Funding
Abstract
FtsK is a hexameric DNA translocase that participates in the final stages of bacterial chromosome segregation. Here we investigate the DNA-binding and translocation activities of FtsK in real time by imaging fluorescently tagged proteins on nanofabricated curtains of DNA. We show that FtsK preferentially loads at 8-bp KOPS (FtsK Orienting Polar Sequences) sites and that loading is enhanced in the presence of ADP. We also demonstrate that FtsK locates KOPS through a mechanism that does not involve extensive 1D diffusion at the scale of our resolution. Upon addition of ATP, KOPS-bound FtsK translocates in the direction dictated by KOPS polarity, and once FtsK has begun translocating it does not rerecognize KOPS from either direction. However, FtsK can abruptly change directions while translocating along DNA independent of KOPS, suggesting that the ability to reorient on DNA does not arise from DNA sequence-specific effects. Taken together, our data support a model in which FtsK locates KOPS through random collisions, preferentially engages KOPS in the ADP-bound state, translocates in the direction dictated by the polar orientation of KOPS, and is incapable of recognizing KOPS while translocating along DNA.
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