ArticleNucleic acids research2012
The orientation of the C-terminal domain of the Saccharomyces cerevisiae Rap1 protein is determined by its binding to DNA.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Ctf18-dependent localization of interstitial telomeric sequence to nuclear pore complexes prevents chromosome fragility.Nucleic acids research · 2026Article
- Restriction of Ku translocation protects telomere ends.Nature communications · 2025Article
- The DNA damage tolerance factor Rad5 and telomere replication.Current genetics · 2025Review
- Unwrap RAP1's Mystery at Kinetoplastid Telomeres.Biomolecules · 2024Review
- DNA binding modes influence Rap1 activity in the regulation of telomere length and MRX functions at DNA ends.Nucleic acids research · 2020Article
- 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
- Either Rap1 or Cdc13 can protect telomeric single-stranded 3' overhangs from degradation in vitro.Scientific reports · 2019Article
- Shepherding DNA ends: Rif1 protects telomeres and chromosome breaks.Microbial cell (Graz, Austria) · 2018Review
- Rap1 and Cdc13 have complementary roles in preventing exonucleolytic degradation of telomere 5' ends.Scientific reports · 2017Article
- Identification of a transcriptional activation domain in yeast repressor activator protein 1 (Rap1) using an altered DNA-binding specificity variant.The Journal of biological chemistry · 2017Article
- Pif1 removes a Rap1-dependent barrier to the strand displacement activity of DNA polymerase δ.Nucleic acids research · 2016Article
- ChEC-seq kinetics discriminates transcription factor binding sites by DNA sequence and shape in vivo.Nature communications · 2015Article
- The wrapping loop and Rap1 C-terminal (RCT) domain of yeast Rap1 modulate access to different DNA binding modes.The Journal of biological chemistry · 2015Article
- 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
- Molecular dissection of the genetic mechanisms that underlie expression conservation in orthologous yeast ribosomal promoters.Genome research · 2014Article
- End-joining inhibition at telomeres requires the translocase and polySUMO-dependent ubiquitin ligase Uls1.The EMBO journal · 2013Article
- One identity or more for telomeres?Frontiers in oncology · 2013Article
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Authors and funding
12 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rap1 is an essential DNA-binding factor from the yeast Saccharomyces cerevisiae involved in transcription and telomere maintenance. Its binding to DNA targets Rap1 at particular loci, and may optimize its ability to form functional macromolecular assemblies. It is a modular protein, rich in large potentially unfolded regions, and comprising BRCT, Myb and RCT well-structured domains. Here, we present the architectures of Rap1 and a Rap1/DNA complex, built through a step-by-step integration of small angle X-ray scattering, X-ray crystallography and nuclear magnetic resonance data. Our results reveal Rap1 structural adjustment upon DNA binding that involves a specific orientation of the C-terminal (RCT) domain with regard to the DNA binding domain (DBD). Crystal structure of DBD in complex with a long DNA identifies an essential wrapping loop, which constrains the orientation of the RCT and affects Rap1 affinity to DNA. Based on our structural information, we propose a model for Rap1 assembly at telomere.
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