ArticleGenes & development2009
Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres.
Article in Genes & development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
92 citing papers in PubMed, 130 citations in OpenAlex.
- The yeast CST and Polα/primase complexes act in concert to ensure proper telomere maintenance and protection.Nucleic acids research · 2025Article
- RPA-like single-stranded DNA-binding protein complexes including CST serve as specialized processivity factors for polymerases.Current opinion in structural biology · 2023Review
- Multiple intermolecular interactions facilitate rapid evolution of essential genes.Nature ecology & evolution · 2023Article
- Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021Review
- OB-Folds and Genome Maintenance: Targeting Protein-DNA Interactions for Cancer Therapy.Cancers · 2021Review
- CST in maintaining genome stability: Beyond telomeres.DNA repair · 2021Review
- Prediction of HIV drug resistance based on the 3D protein structure: Proposal of molecular field mapping.PloS one · 2021Article
- Telomere Replication: Solving Multiple End Replication Problems.Frontiers in cell and developmental biology · 2021Review
- Article
- Structural insights into telomere protection and homeostasis regulation by yeast CST complex.Nature structural & molecular biology · 2020Article
- Role of folding kinetics of secondary structures in telomeric G-overhangs in the regulation of telomere maintenance inThe Journal of biological chemistry · 2020Article
- Roles of OB-Fold Proteins in Replication Stress.Frontiers in cell and developmental biology · 2020Review
- Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020Review
- Review
- Back to the future: The intimate and evolving connection between telomere-related factors and genotoxic stress.The Journal of biological chemistry · 2019Review
- Mammalian CST averts replication failure by preventing G-quadruplex accumulation.Nucleic acids research · 2019Article
- Review
- Tpz1Communications biology · 2019Article
- Single-stranded telomere-binding protein employs a dual rheostat for binding affinity and specificity that drives function.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Shieldin complex promotes DNA end-joining and counters homologous recombination in BRCA1-null cells.Nature cell biology · 2018Article
32 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
In budding yeast, Cdc13, Stn1, and Ten1 form a heterotrimeric complex (CST) that is essential for telomere protection and maintenance. Previous bioinformatics analysis revealed a putative oligonucleotide/oligosaccharide-binding (OB) fold at the N terminus of Stn1 (Stn1N) that shows limited sequence similarity to the OB fold of Rpa2, a subunit of the eukaryotic ssDNA-binding protein complex replication protein A (RPA). Here we present functional and structural analyses of Stn1 and Ten1 from multiple budding and fission yeast. The crystal structure of the Candida tropicalis Stn1N complexed with Ten1 demonstrates an Rpa2N-Rpa3-like complex. In both structures, the OB folds of the two components pack against each other through interactions between two C-terminal helices. The structure of the C-terminal domain of Saccharomyces cerevisiae Stn1 (Stn1C) was found to comprise two related winged helix-turn-helix (WH) motifs, one of which is most similar to the WH motif at the C terminus of Rpa2, again supporting the notion that Stn1 resembles Rpa2. The crystal structure of the fission yeast Schizosaccharomyces pombe Stn1N-Ten1 complex exhibits a virtually identical architecture as the C. tropicalis Stn1N-Ten1. Functional analyses of the Candida albicans Stn1 and Ten1 proteins revealed critical roles for these proteins in suppressing aberrant telomerase and recombination activities at telomeres. Mutations that disrupt the Stn1-Ten1 interaction induce telomere uncapping and abolish the telomere localization of Ten1. Collectively, our structural and functional studies illustrate that, instead of being confined to budding yeast telomeres, the CST complex may represent an evolutionarily conserved RPA-like telomeric complex at the 3' overhangs that works in parallel with or instead of the well-characterized POT1-TPP1/TEBPalpha-beta complex.
Indexed as
Identifiers
What OpenQuestion holds
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.