ArticleNucleic acids research2012
The N-terminus of the human RecQL4 helicase is a homeodomain-like DNA interaction motif.
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 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Review
- RECQL4 requires PARP1 for recruitment to DNA damage, and PARG dePARylation facilitates its associated role in end joining.Experimental & molecular medicine · 2025Article
- HROB Is Implicated in DNA Replication.Genes · 2024Article
- A Chinese patient with Rothmund-Thomson syndrome.Molecular genetics & genomic medicine · 2024Article
- Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase.Nature communications · 2023Article
- DONSON facilitates Cdc45 and GINS chromatin association and is essential for DNA replication initiation.Nucleic acids research · 2023Article
- Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1.DNA repair · 2021Review
- Molecular Mechanisms of the RECQ4 Pathogenic Mutations.Frontiers in molecular biosciences · 2021Review
- The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism.Nature communications · 2017Article
- Yeast Hrq1 shares structural and functional homology with the disease-linked human RecQ4 helicase.Nucleic acids research · 2017Article
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- Ribosomal Protein S3 Negatively Regulates Unwinding Activity of RecQ-like Helicase 4 through Their Physical Interaction.The Journal of biological chemistry · 2017Article
- Review
- Multi-BRCT scaffolds use distinct strategies to support genome maintenance.Cell cycle (Georgetown, Tex.) · 2016Review
- Structural and biochemical characterization of an RNA/DNA binding motif in the N-terminal domain of RecQ4 helicases.Scientific reports · 2016Article
- Interaction of RECQ4 and MCM10 is important for efficient DNA replication origin firing in human cells.Oncotarget · 2015Article
- Evolutionary conservation of the CDK targets in eukaryotic DNA replication initiation.Chromosoma · 2015Review
- Insights into the Initiation of Eukaryotic DNA Replication.Nucleus (Austin, Tex.) · 2015Article
- The intrinsically disordered amino-terminal region of human RecQL4: multiple DNA-binding domains confer annealing, strand exchange and G4 DNA binding.Nucleic acids research · 2014Article
- CDK phosphorylation of SLD-2 is required for replication initiation and germline development in C. elegans.The Journal of cell biology · 2014Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RecQL4 helicase is involved in the maintenance of genome integrity and DNA replication. Mutations in the human RecQL4 gene cause the Rothmund-Thomson, RAPADILINO and Baller-Gerold syndromes. Mouse models and experiments in human and Xenopus have proven the N-terminal part of RecQL4 to be vital for cell growth. We have identified the first 54 amino acids of RecQL4 (RecQL4_N54) as the minimum interaction region with human TopBP1. The solution structure of RecQL4_N54 was determined by heteronuclear liquid-state nuclear magnetic resonance (NMR) spectroscopy (PDB 2KMU; backbone root-mean-square deviation 0.73 Å). Despite low-sequence homology, the well-defined structure carries an overall helical fold similar to homeodomain DNA-binding proteins but lacks their archetypical, minor groove-binding N-terminal extension. Sequence comparison indicates that this N-terminal homeodomain-like fold is a common hallmark of metazoan RecQL4 and yeast Sld2 DNA replication initiation factors. RecQL4_N54 binds DNA without noticeable sequence specificity yet with apparent preference for branched over double-stranded (ds) or single-stranded (ss) DNA. NMR chemical shift perturbation observed upon titration with Y-shaped, ssDNA and dsDNA shows a major contribution of helix α3 to DNA binding, and additional arginine side chain interactions for the ss and Y-shaped DNA.
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