ArticleNucleic acids research2010
Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- R-loops and D-loops: a delicate balance in genomic stability and instability.Cell communication and signaling : CCS · 2026Review
- Telomeres as hotspots for innate immunity and inflammation.DNA repair · 2024Review
- Homology directed telomere clustering, ultrabright telomere formation and nuclear envelope rupture in cells lacking TRF2Nature communications · 2023Article
- Rap1 regulates TIP60 function during fate transition between two-cell-like and pluripotent states.Genes & development · 2022Article
- TIN2 is an architectural protein that facilitates TRF2-mediated trans- and cis-interactions on telomeric DNA.Nucleic acids research · 2021Article
- TRF2 promotes dynamic and stepwise looping of POT1 bound telomeric overhang.Nucleic acids research · 2021Article
- Review
- Review
- Telomeres and Cancer: Resolving the Paradox.Annual review of cancer biology · 2021Article
- Roles for the 8-Oxoguanine DNA Repair System in Protecting Telomeres From Oxidative Stress.Frontiers in cell and developmental biology · 2021Review
- To Join or Not to Join: Decision Points Along the Pathway to Double-Strand Break Repair vs. Chromosome End Protection.Frontiers in cell and developmental biology · 2021Review
- Recent Advances in Understanding Werner Syndrome.F1000Research · 2017Review
- TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions.Nature communications · 2016Article
- Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2.Scientific reports · 2016Article
- The DNA structure and sequence preferences of WRN underlie its function in telomeric recombination events.Nature communications · 2015Article
- Human Rap1 modulates TRF2 attraction to telomeric DNA.Nucleic acids research · 2015Article
- Novel function of the Fanconi anemia group J or RECQ1 helicase to disrupt protein-DNA complexes in a replication protein A-stimulated manner.The Journal of biological chemistry · 2014Article
- Strand exchange of telomeric DNA catalyzed by the Werner syndrome protein (WRN) is specifically stimulated by TRF2.Nucleic acids research · 2014Article
- Human RECQL1 participates in telomere maintenance.Nucleic acids research · 2014Article
- TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
WRN protein loss causes Werner syndrome (WS), which is characterized by premature aging as well as genomic and telomeric instability. WRN prevents telomere loss, but the telomeric protein complex must regulate WRN activities to prevent aberrant telomere processing. Telomere-binding TRF2 protein inhibits telomere t-loop deletion by blocking Holliday junction (HJ) resolvase cleavage activity, but whether TRF2 also modulates HJ displacement at t-loops is unknown. In this study, we used multiplex fluorophore imaging to track the fate of individual strands of HJ substrates. We report the novel finding that TRF2 inhibits WRN helicase strand displacement of HJs with telomeric repeats in duplex arms, but unwinding of HJs with a telomeric center or lacking telomeric sequence is unaffected. These data, together with results using TRF2 fragments and TRF2 HJ binding assays, indicate that both the TRF2 B- and Myb domains are required to inhibit WRN HJ activity. We propose a novel model whereby simultaneous binding of the TRF2 B-domain to the HJ core and the Myb domain to telomeric arms promote and stabilize HJs in a stacked arm conformation that is unfavorable for unwinding. Our biochemical study provides a mechanistic basis for the cellular findings that TRF2 regulates WRN activity at telomeres.
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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.