ArticleAging2012
DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities.
Article in Aging, 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, 30 citations in OpenAlex.
- Review
- Article
- Response to Replication Stress and Maintenance of Genome Stability by WRN, the Werner Syndrome Protein.International journal of molecular sciences · 2024Review
- CDK2 phosphorylation of Werner protein (WRN) contributes to WRN's DNA double-strand break repair pathway choice.Aging cell · 2021Article
- Comparative Analysis of Mammal Genomes Unveils Key Genomic Variability for Human Life Span.Molecular biology and evolution · 2021Article
- Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021Review
- Acidic domain of WRNp is critical for autophagy and up-regulates age associated proteins.DNA repair · 2018Article
- The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism.Nature communications · 2017Article
- WRN is recruited to damaged telomeres via its RQC domain and tankyrase1-mediated poly-ADP-ribosylation of TRF1.Nucleic acids research · 2017Article
- Werner syndrome: Clinical features, pathogenesis and potential therapeutic interventions.Ageing research reviews · 2017Review
- WRN Mutation Update: Mutation Spectrum, Patient Registries, and Translational Prospects.Human mutation · 2017Review
- WRN regulates pathway choice between classical and alternative non-homologous end joining.Nature communications · 2016Article
- Differential and Concordant Roles for Poly(ADP-Ribose) Polymerase 1 and Poly(ADP-Ribose) in Regulating WRN and RECQL5 Activities.Molecular and cellular biology · 2015Article
- Human RECQL1 participates in telomere maintenance.Nucleic acids research · 2014Article
- A nucleotide-dependent and HRDC domain-dependent structural transition in DNA-bound RecQ helicase.The Journal of biological chemistry · 2014Article
- Human RecQ helicases in DNA repair, recombination, and replication.Annual review of biochemistry · 2014Review
- Structural mechanisms of human RecQ helicases WRN and BLM.Frontiers in genetics · 2014Review
- Catalytic activities of Werner protein are affected by adduction with 4-hydroxy-2-nonenal.Nucleic acids research · 2014Article
- Structure of the RecQ C-terminal domain of human Bloom syndrome protein.Scientific reports · 2013Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Werner protein (WRN), member of the RecQ helicase family, is a helicase and exonuclease, and participates in multiple DNA metabolic processes including DNA replication, recombination and DNA repair. Mutations in the WRN gene cause Werner syndrome, associated with premature aging, genome instability and cancer predisposition. The RecQ C-terminal (RQC) domain of WRN, containing α2-α3 loop and β-wing motifs, is important for DNA binding and for many protein interactions. To better understand the critical functions of this domain, we generated recombinant WRN proteins (using a novel purification scheme) with mutations in Arg-993 within the α2-α3 loop of the RQC domain and in Phe-1037 of the -wing motif. We then studied the catalytic activities and DNA binding of these mutant proteins as well as some important functional protein interactions. The mutant proteins were defective in DNA binding and helicase activity, and interestingly, they had deficient exonuclease activity and strand annealing function. The RQC domain of WRN has not previously been implicated in exonuclease or annealing activities. The mutant proteins could not stimulate NEIL1 incision activity as did the wild type. Thus, the Arg-993 and Phe-1037 in the RQC domain play essential roles in catalytic activity, and in functional interactions mediated by WRN.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.