ArticleBMC structural biology2009
Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm.
Article in BMC structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 37 citations in OpenAlex.
- HELQ & Hel308: ancient enzymes of DNA repair and recombination.Biochemical Society transactions · 2026Review
- Helicase HELQ: Molecular Characters Fit for DSB Repair Function.International journal of molecular sciences · 2024Review
- Archaeal Hel308 suppresses recombination through a catalytic switch that controls DNA annealing.Nucleic acids research · 2023Article
- Genome Protection by DNA Polymerase θ.Annual review of genetics · 2022Review
- Review
- A deep dive into the RecQ interactome: something old and something new.Current genetics · 2021Review
- Taking a molecular motor for a spin: helicase mechanism studied by spin labeling and PELDOR.Nucleic acids research · 2016Article
- Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway.Structure (London, England : 1993) · 2015Article
- The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding.Nucleic acids research · 2014Article
- End resection at double-strand breaks: mechanism and regulation.Cold Spring Harbor perspectives in biology · 2014Review
- Nanobiomotors of archaeal DNA repair machineries: current research status and application potential.Cell & bioscience · 2014Review
- Helq acts in parallel to Fancc to suppress replication-associated genome instability.Nucleic acids research · 2013Article
- Ski2-like RNA helicase structures: common themes and complex assemblies.RNA biology · 2013Review
- Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing.Molecular bioSystems · 2012Article
- A novel missense SNRNP200 mutation associated with autosomal dominant retinitis pigmentosa in a Chinese family.PloS one · 2012Article
- Review
- Characterization of metalloproteins by high-throughput X-ray absorption spectroscopy.Genome research · 2011Article
- Prp43p contains a processive helicase structural architecture with a specific regulatory domain.The EMBO journal · 2010Article
- The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing.The EMBO journal · 2010Article
- Structural basis for the function of DEAH helicases.EMBO reports · 2010Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPyrococcus furiosus Hjm (PfuHjm) is a structure-specific DNA helicase that was originally identified by in vitro screening for Holliday junction migration activity. It belongs to helicase superfamily 2, and shares homology with the human DNA polymerase Theta (PolTheta), HEL308, and Drosophila Mus308 proteins, which are involved in DNA repair. Previous biochemical and genetic analyses revealed that PfuHjm preferentially binds to fork-related Y-structured DNAs and unwinds their double-stranded regions, suggesting that this helicase is a functional counterpart of the bacterial RecQ helicase, which is essential for genome maintenance. Elucidation of the DNA unwinding and translocation mechanisms by PfuHjm will require its three-dimensional structure at atomic resolution.
resultsWe determined the crystal structures of PfuHjm, in two apo-states and two nucleotide bound forms, at resolutions of 2.0-2.7 A. The overall structures and the local conformations around the nucleotide binding sites are almost the same, including the side-chain conformations, irrespective of the nucleotide-binding states. The architecture of Hjm was similar to that of Archaeoglobus fulgidus Hel308 complexed with DNA. An Hjm-DNA complex model, constructed by fitting the five domains of Hjm onto the corresponding Hel308 domains, indicated that the interaction of Hjm with DNA is similar to that of Hel308. Notably, sulphate ions bound to Hjm lie on the putative DNA binding surfaces. Electron microscopic analysis of an Hjm-DNA complex revealed substantial flexibility of the double stranded region of DNA, presumably due to particularly weak protein-DNA interactions. Our present structures allowed reasonable homology model building of the helicase region of human PolTheta, indicating the strong conformational conservation between archaea and eukarya.
conclusionThe detailed comparison between our DNA-free PfuHjm structure and the structure of Hel308 complexed with DNA suggests similar DNA unwinding and translocation mechanisms, which could be generalized to all of the members in the same family. Structural comparison also implied a minor rearrangement of the five domains during DNA unwinding reaction. The unexpected small contact between the DNA duplex region and the enzyme appears to be advantageous for processive helicase activity.
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