ArticleThe Journal of biological chemistry2010
Characterization of the yeast telomere nucleoprotein core: Rap1 binds independently to each recognition site.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Phage-encoded TelN inhibits bacterial Mre11-Rad50 nuclease to protect hairpin telomeres.The EMBO journal · 2025Article
- Restriction of Ku translocation protects telomere ends.Nature communications · 2025Article
- The DNA damage tolerance factor Rad5 and telomere replication.Current genetics · 2025Review
- Telomerase gene therapy: a remission toward cancer.Medical oncology (Northwood, London, England) · 2022Review
- Chromatin Fiber Invasion and Nucleosome Displacement by the Rap1 Transcription Factor.Molecular cell · 2020Article
- Rap1-mediated nucleosome displacement can regulate gene expression in senescent cells without impacting the pace of senescence.Aging cell · 2020Article
- The telomere-binding protein Rif2 and ATP-bound Rad50 have opposing roles in the activation of yeast Tel1The Journal of biological chemistry · 2019Article
- Article
- Alternative arrangements of telomeric recognition sites regulate the binding mode of the DNA-binding domain of yeast Rap1.Biophysical chemistry · 2015Article
- The DNA-binding domain of yeast Rap1 interacts with double-stranded DNA in multiple binding modes.Biochemistry · 2014Article
- Coordinated interactions of multiple POT1-TPP1 proteins with telomere DNA.The Journal of biological chemistry · 2013Article
- End-joining inhibition at telomeres requires the translocase and polySUMO-dependent ubiquitin ligase Uls1.The EMBO journal · 2013Article
- The orientation of the C-terminal domain of the Saccharomyces cerevisiae Rap1 protein is determined by its binding to DNA.Nucleic acids research · 2012Article
- Rap1 binds single-stranded DNA at telomeric double- and single-stranded junctions and competes with Cdc13 protein.The Journal of biological chemistry · 2011Article
- Single- and double-stranded DNA binding proteins act in concert to conserve a telomeric DNA core sequence.Genome integrity · 2011Article
- Potential Risks in the Paradigm of Basic to Translational Research: A Critical Evaluation of qPCR Telomere Size Techniques.Journal of cancer epidemiology & treatmentArticle
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
At the core of Saccharomyces cerevisiae telomeres is an array of tandem telomeric DNA repeats bound site-specifically by multiple Rap1 molecules. There, Rap1 orchestrates the binding of additional telomere-associated proteins and negatively regulates both telomere fusion and length homeostasis. Using electron microscopy, viscosity, and light scattering measurements, we show that purified Rap1 is a monomer in solution that adopts a ringlike or C shape with a central cavity. Rap1 could orchestrate telomere function by binding multiple telomere array sites through either cooperative or independent mechanisms. To determine the mechanism, we analyze the distribution of Rap1 monomers on defined telomeric DNA arrays. This analysis clearly indicates that Rap1 binds independently to each nonoverlapping site in an array, regardless of the spacing between sites, the total number of sites, the affinity of the sites for Rap1, and over a large concentration range. Previous experiments have not clearly separated the effects of affinity from repeat spacing on telomere function. We clarify these results by testing in vivo the function of defined telomere arrays containing the same Rap1 binding site separated by spacings that were previously defined as low or high activity. We find that Rap1 binding affinity in vitro correlates with the ability of telomeric repeat arrays to regulate telomere length in vivo. We suggest that Rap1 binding to multiple sites in a telomere array does not, by itself, promote formation of a more energetically stabile complex.
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