ArticleThe Journal of biological chemistry2010
Multiple Escherichia coli RecQ helicase monomers cooperate to unwind long DNA substrates: a fluorescence cross-correlation spectroscopy study.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 21 citations in OpenAlex.
- The transitional kinetics between open and closed Rep structures can be tuned by salt via two intermediate states.Nucleic acids research · 2026Article
- Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights fromInternational journal of molecular sciences · 2021Review
- The HRDC domain oppositely modulates the unwinding activity of E. coli RecQ helicase on duplex DNA and G-quadruplex.The Journal of biological chemistry · 2020Article
- Interplay between Cellular Uptake, Intracellular Localization and the Cell Death Mechanism in Triphenylamine-Mediated Photoinduced Cell Death.Scientific reports · 2020Article
- Mechanistic insight into cadmium-induced inactivation of the Bloom protein.Scientific reports · 2016Article
- Single-molecule visualization of RecQ helicase reveals DNA melting, nucleation, and assembly are required for processive DNA unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Fine tuning of a DNA fork by the RecQ helicase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The Bacteroides sp. 3_1_23 Pif1 protein is a multifunctional helicase.Nucleic acids research · 2015Article
- Screening for FtsZ Dimerization Inhibitors Using Fluorescence Cross-Correlation Spectroscopy and Surface Resonance Plasmon Analysis.PloS one · 2015Article
- Insight into the cooperative DNA binding of the O⁶-alkylguanine DNA alkyltransferase.DNA repair · 2014Review
- A nucleotide-dependent and HRDC domain-dependent structural transition in DNA-bound RecQ helicase.The Journal of biological chemistry · 2014Article
- Tight intramolecular regulation of the human Upf1 helicase by its N- and C-terminal domains.Nucleic acids research · 2013Article
- RecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical coupling.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster.Nucleic acids research · 2012Review
- SF1 and SF2 helicases: family matters.Current opinion in structural biology · 2010Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RecQ family helicases catalyze the DNA unwinding reaction in an ATP hydrolysis-dependent manner. We investigated the mechanism of DNA unwinding by the Escherichia coli RecQ helicase using a new sensitive helicase assay based on fluorescence cross-correlation spectroscopy (FCCS) with two-photon excitation. The FCCS-based assay can be used to measure the unwinding activity under both single and multiple turnover conditions with no limitation related to the size of the DNA strands constituting the DNA substrate. We found that the monomeric helicase was sufficient to perform the unwinding of short DNA substrates. However, a significant increase in the activity was observed using longer DNA substrates, under single turnover conditions, originating from the simultaneous binding of multiple helicase monomers to the same DNA molecule. This functional cooperativity was strongly dependent on several factors, including DNA substrate length, the number and size of single-stranded 3'-tails, and the temperature. Regarding the latter parameter, a strong cooperativity was observed at 37 degrees C, whereas only modest or no cooperativity was observed at 25 degrees C regardless of the nature of the DNA substrate. Consistently, the functional cooperativity was found to be tightly associated with a cooperative DNA binding mode. We also showed that the cooperative binding of helicase to the DNA substrate indirectly accounts for the sigmoidal dependence of unwinding activity on ATP concentration, which also occurs only at 37 degrees C but not at 25 degrees C. Finally, we further examined the influences of spontaneous DNA rehybridization (after helicase translocation) and the single-stranded DNA binding property of helicase on the unwinding activity as detected in the FCCS assay.
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