ArticleBiophysical journal2013
Single-molecule imaging of the oligomer formation of the nonhexameric Escherichia coli UvrD helicase.
Article in Biophysical journal, 2013. 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, 40 citations in OpenAlex.
- Structural basis for dimerization and activation of UvrD-family helicases.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024Review
- Structural Basis for Dimerization and Activation of UvrD-family Helicases.bioRxiv : the preprint server for biology · 2024Article
- Subunit Communication within Dimeric SF1 DNA Helicases.Journal of molecular biology · 2024Article
- Article
- Quantitative and kinetic single-molecule analysis of DNA unwinding byBiophysics and physicobiology · 2022Article
- Optical tweezer and TIRF microscopy for single molecule manipulation of RNA/DNA nanostructures including their rubbery property and single molecule counting.Biophysics reports · 2021Article
- Heterogeneous dissociation process of truncated RNAs by oligomerized Vasa helicase.Communications biology · 2021Article
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights fromInternational journal of molecular sciences · 2021Review
- Bacterial Vivisection: How Fluorescence-Based Imaging Techniques Shed a Light on the Inner Workings of Bacteria.Microbiology and molecular biology reviews : MMBR · 2020Review
- DNA-Unwinding Dynamics of Escherichia coli UvrD Lacking the C-Terminal 40 Amino Acids.Biophysical journal · 2020Article
- Overview of the "1SBA: integrative approaches towards understanding of gene expression" session at the 57th BSJ meeting.Biophysical reviews · 2020Article
- Rep and UvrD Antagonize One Another at Stalled Replication Forks and This Is Exacerbated by SSB.ACS omega · 2019Article
- Regulation of Rep helicase unwinding by an auto-inhibitory subdomain.Nucleic acids research · 2019Article
- Regulation of UvrD Helicase Activity by MutL.Journal of molecular biology · 2018Article
- Large domain movements upon UvrD dimerization and helicase activation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Taking a molecular motor for a spin: helicase mechanism studied by spin labeling and PELDOR.Nucleic acids research · 2016Article
- Synergistic effect of ATP for RuvA-RuvB-Holliday junction DNA complex formation.Scientific reports · 2015Article
- Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme.Science (New York, N.Y.) · 2015Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Superfamily I helicases are nonhexameric helicases responsible for the unwinding of nucleic acids. However, whether they unwind DNA in the form of monomers or oligomers remains a controversy. In this study, we addressed this question using direct single-molecule fluorescence visualization of Escherichia coli UvrD, a superfamily I DNA helicase. We performed a photobleaching-step analysis of dye-labeled helicases and determined that the helicase is bound to 18-basepair (bp) double-stranded DNA (dsDNA) with a 3' single-stranded DNA (ssDNA) tail (12, 20, or 40 nt) in a dimeric or trimeric form in the absence of ATP. We also discovered through simultaneous visualization of association/dissociation of the helicase with/from DNA and the DNA unwinding dynamics of the helicase in the presence of ATP that these dimeric and trimeric forms are responsible for the unwinding of DNA. We can therefore propose a new kinetic scheme for the helicase-DNA interaction in which not only a dimeric helicase but also a trimeric helicase can unwind DNA. This is, to our knowledge, the first direct single-molecule nonhexameric helicase quantification study, and it strongly supports a model in which an oligomer is the active form of the helicase, which carries important implications for the DNA unwinding mechanism of all superfamily I helicases.
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