ArticleJournal of molecular biology2012
Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- A conserved mechanism for dimerization and activation of superfamily 1A UvrD-family helicases.Nucleic acids research · 2026Article
- ClpA- and ClpAP-catalyzed unfolding and translocation are differentially coupled to ATP binding.Biophysical journal · 2026Article
- Article
- Kinetic and structural mechanism for DNA unwinding by a non-hexameric helicase.Nature communications · 2021Article
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Regulation of E. coli Rep helicase activity by PriC.Journal of molecular biology · 2021Article
- Remodeler Catalyzed Nucleosome Repositioning: Influence of Structure and Stability.International journal of molecular sciences · 2020Review
- UvrD helicase activation by MutL involves rotation of its 2B subdomain.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Protein Environment and DNA Orientation Affect Protein-Induced Cy3 Fluorescence Enhancement.Biophysical journal · 2019Article
- Large domain movements upon UvrD dimerization and helicase activation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Modulation of Escherichia coli UvrD Single-Stranded DNA Translocation by DNA Base Composition.Biophysical journal · 2017Article
- Monitoring Replication Protein A (RPA) dynamics in homologous recombination through site-specific incorporation of non-canonical amino acids.Nucleic acids research · 2017Article
- Methods to study the coupling between replicative helicase and leading-strand DNA polymerase at the replication fork.Methods (San Diego, Calif.) · 2016Review
- Processive DNA Unwinding by RecBCD Helicase in the Absence of Canonical Motor Translocation.Journal of molecular biology · 2016Article
- Chemo-mechanical pushing of proteins along single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Active displacement of RecA filaments by UvrD translocase activity.Nucleic acids research · 2015Article
- Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme.Science (New York, N.Y.) · 2015Article
- The UvrD303 hyper-helicase exhibits increased processivity.The Journal of biological chemistry · 2014Article
- Recombination hotspots attenuate the coupled ATPase and translocase activities of an AddAB-type helicase-nuclease.Nucleic acids research · 2014Article
- Single-molecule imaging of the oligomer formation of the nonhexameric Escherichia coli UvrD helicase.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Escherichia coli UvrD is an SF1A (superfamily 1 type A) helicase/translocase that functions in several DNA repair pathways. A UvrD monomer is a rapid and processive single-stranded DNA (ssDNA) translocase but is unable to unwind DNA processively in vitro. Based on data at saturating ATP (500 μM), we proposed a nonuniform stepping mechanism in which a UvrD monomer translocates with biased (3' to 5') directionality while hydrolyzing 1 ATP per DNA base translocated, but with a kinetic step size of 4-5 nt/step, suggesting that a pause occurs every 4-5 nt translocated. To further test this mechanism, we examined UvrD translocation over a range of lower ATP concentrations (10-500 μM ATP), using transient kinetic approaches. We find a constant ATP coupling stoichiometry of ∼1 ATP/DNA base translocated even at the lowest ATP concentration examined (10 μM), indicating that ATP hydrolysis is tightly coupled to forward translocation of a UvrD monomer along ssDNA with little slippage or futile ATP hydrolysis during translocation. The translocation kinetic step size remains constant at 4-5 nt/step down to 50 μM ATP but increases to ∼7 nt/step at 10 μM ATP. These results suggest that UvrD pauses more frequently during translocation at low ATP but with little futile ATP hydrolysis.
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