ArticleThe Journal of biological chemistry2015
The wrapping loop and Rap1 C-terminal (RCT) domain of yeast Rap1 modulate access to different DNA binding modes.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- DecodingbioRxiv : the preprint server for biology · 2025Article
- Article
- To Fix or Not to Fix: Maintenance of Chromosome Ends Versus Repair of DNA Double-Strand Breaks.Cells · 2022Review
- Novel insights into the mechanism of cell cycle kinases Mec1(ATR) and Tel1(ATM).Critical reviews in biochemistry and molecular biology · 2021Article
- DNA binding modes influence Rap1 activity in the regulation of telomere length and MRX functions at DNA ends.Nucleic acids research · 2020Article
- Either Rap1 or Cdc13 can protect telomeric single-stranded 3' overhangs from degradation in vitro.Scientific reports · 2019Article
- Repression of Divergent Noncoding Transcription by a Sequence-Specific Transcription Factor.Molecular cell · 2018Article
- Rap1 and Cdc13 have complementary roles in preventing exonucleolytic degradation of telomere 5' ends.Scientific reports · 2017Article
- Double-stranded telomeric DNA binding proteins: Diversity matters.Cell cycle (Georgetown, Tex.) · 2017Review
- Pif1 removes a Rap1-dependent barrier to the strand displacement activity of DNA polymerase δ.Nucleic acids research · 2016Article
- Evolution and Functional Trajectory of Sir1 in Gene Silencing.Molecular and cellular biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Budding yeast Rap1 is a specific double-stranded DNA-binding protein involved in repression and activation of gene transcription and in the establishment of the nucleoprotein complex formed at telomeres. The DNA-binding domain (DBD) of Rap1 forms a high affinity complex with DNA where both Myb-like domains bind to the recognition site. However, we recently showed that the DBD can also access an alternative, lower affinity DNA-binding mode where a single Myb-like domain binds. This results in Rap1-DNA complexes with stoichiometry higher than previously anticipated. In this work, we show that the ability of the DBD to form higher stoichiometry complexes on DNA is maintained also in larger Rap1 constructs. This indicates that transition between at least two DNA-binding modes is a general property of the protein and not a specific feature of the DBD in isolation. The transition between binding modes is modulated by the C-terminal wrapping loop within the DBD, consistent with the proposed model in which the transient opening of this region allows a switch between binding modes. Finally, we provide evidence that the Rap1 C terminus interacts with the DNA-binding domain, suggesting a complex network of interactions that couples changes in conformation of the protein to the binding of its DNA recognition sequence.
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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.