ArticleNucleic acids research2012
Complex activities of the human Bloom's syndrome helicase are encoded in a core region comprising the RecA and Zn-binding domains.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Shuttling of RecQ helicase HIM-6 coordinates iterative cycle of unwinding, pulling, and backsliding.Nucleic acids research · 2026Article
- The toposiomerase IIIalpha-RMI1-RMI2 complex orients human Bloom's syndrome helicase for efficient disruption of D-loops.Nature communications · 2022Article
- Evaluation and modulation of DNA lesion bypass in an SV40 large T antigen-based in vitro replication system.FEBS open bio · 2021Article
- Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021Review
- Single molecule kinetics uncover roles for E. coli RecQ DNA helicase domains and interaction with SSB.Nucleic acids research · 2018Article
- RecQ helicase triggers a binding mode change in the SSB-DNA complex to efficiently initiate DNA unwinding.Nucleic acids research · 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
- Site-directed mutants of human RECQ1 reveal functional importance of the zinc binding domain.Mutation research · 2016Article
- Mechanistic insight into cadmium-induced inactivation of the Bloom protein.Scientific reports · 2016Article
- Cellular defects caused by hypomorphic variants of the Bloom syndrome helicase gene BLM.Molecular genetics & genomic medicine · 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
- The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling.Scientific reports · 2015Article
- Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes.Nucleic acids research · 2015Article
- Molecular mechanism of double Holliday junction dissolution.Cell & bioscience · 2014Review
- Structure of the RecQ C-terminal domain of human Bloom syndrome protein.Scientific reports · 2013Article
- Fork sensing and strand switching control antagonistic activities of RecQ helicases.Nature communications · 2013Article
- DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities.Aging · 2012Article
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6 authors.
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Abstract
Bloom's syndrome DNA helicase (BLM), a member of the RecQ family, is a key player in homologous recombination (HR)-based error-free DNA repair processes. During HR, BLM exerts various biochemical activities including single-stranded (ss) DNA translocation, separation and annealing of complementary DNA strands, disruption of complex DNA structures (e.g. displacement loops) and contributes to quality control of HR via clearance of Rad51 nucleoprotein filaments. We performed a quantitative mechanistic analysis of truncated BLM constructs that are shorter than the previously identified minimal functional module. Surprisingly, we found that a BLM construct comprising only the two conserved RecA domains and the Zn(2+)-binding domain (residues 642-1077) can efficiently perform all mentioned HR-related activities. The results demonstrate that the Zn(2+)-binding domain is necessary for functional interaction with DNA. We show that the extensions of this core, including the winged-helix domain and the strand separation hairpin identified therein in other RecQ-family helicases, are not required for mechanochemical activity per se and may instead play modulatory roles and mediate protein-protein interactions.
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