ArticleScientific reports2015
The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- Review
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- The toposiomerase IIIalpha-RMI1-RMI2 complex orients human Bloom's syndrome helicase for efficient disruption of D-loops.Nature communications · 2022Article
- Structure of the helicase core of Werner helicase, a key target in microsatellite instability cancers.Life science alliance · 2021Article
- 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
- RecQ helicases in DNA repair and cancer targets.Essays in biochemistry · 2020Review
- A Toolbox for Site-Specific Labeling of RecQ Helicase With a Single Fluorophore Used in the Single-Molecule Assay.Frontiers in molecular biosciences · 2020Article
- Homology sensing via non-linear amplification of sequence-dependent pausing by RecQ helicase.eLife · 2019Article
- Single molecule kinetics uncover roles for E. coli RecQ DNA helicase domains and interaction with SSB.Nucleic acids research · 2018Article
- Functional fine-tuning between bacterial DNA recombination initiation and quality control systems.PloS one · 2018Article
- RecQ helicase triggers a binding mode change in the SSB-DNA complex to efficiently initiate DNA unwinding.Nucleic acids research · 2017Article
- Force-activated DNA substrates for probing individual proteins interacting with single-stranded DNA.Nucleic acids research · 2017Article
- The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism.Nature communications · 2017Article
- Shuttling along DNA and directed processing of D-loops by RecQ helicase support quality control of homologous recombination.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
DNA-restructuring activities of RecQ-family helicases play key roles in genome maintenance. These activities, driven by two tandem RecA-like core domains, are thought to be controlled by accessory DNA-binding elements including the helicase-and-RnaseD-C-terminal (HRDC) domain. The HRDC domain of human Bloom's syndrome (BLM) helicase was shown to interact with the RecA core, raising the possibility that it may affect the coupling between ATP hydrolysis, translocation along single-stranded (ss)DNA and/or unwinding of double-stranded (ds)DNA. Here, we determined how these activities are affected by the abolition of the ssDNA interaction of the HRDC domain or the deletion of the entire domain in E. coli RecQ helicase. Our data show that the HRDC domain suppresses the rate of DNA-activated ATPase activity in parallel with those of ssDNA translocation and dsDNA unwinding, regardless of the ssDNA binding capability of this domain. The HRDC domain does not affect either the processivity of ssDNA translocation or the tight coupling between the ATPase, translocation, and unwinding activities. Thus, the mechanochemical coupling of E. coli RecQ appears to be independent of HRDC-ssDNA and HRDC-RecA core interactions, which may play roles in more specialized functions of the enzyme.
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