Evidence map›Paper›PMID 24057216›Full record

ArticleNucleic acids research2014

The tenacious recognition of yeast telomere sequence by Cdc13 is fully exerted by a single OB-fold domain.

Karen A Lewis, Danielle A Pfaff, Jennifer N Earley, Sarah E Altschuler, Deborah S Wuttke

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.7field-weighted citation impact, top 28% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. A comprehensive map of hotspots of de novo telomere addition inbioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Telomeres and Cancer.Life (Basel, Switzerland) · 2021
    Review
  10. Review
  11. Article
  12. Roles of OB-Fold Proteins in Replication Stress.Frontiers in cell and developmental biology · 2020
    Review
  13. Review
  14. Article
  15. 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 · 2018
    Article
  16. Article
  17. Emerging roles of CST in maintaining genome stability and human disease.Frontiers in bioscience (Landmark edition) · 2018
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Karen A LewisDepartment of Chemistry and Biochemistry, UCB 543, University of Colorado Boulder, Boulder, CO 80309, USA.
Danielle A Pfaff
Jennifer N Earley
Sarah E Altschuler
Deborah S Wuttke
University of Colorado Boulder · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
SINGLE STRANDED DNA RECOGNITION IN TELOMERESR01GM059414 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI WUTTKE, DEBORAH S. · 1999 to 2015
$3.7M
LEADERSHIP TRAINING IN PHARMACEUTICAL BIOTECHNOLOGYT32GM008732 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI RANDOLPH, THEODORE W · 2001 to 2015
$2.7M
In Vitro Reconstitution and Biochemical Characterization of Yeast TelomeraseF32GM093528 · NIGMS · UNIVERSITY OF COLORADO · PI LEWIS, KAREN ADELL · 2011 to 2012
$105k
NCI NIH HHS P30 CA046934NIGMS NIH HHS GM008732NIGMS NIH HHS GM059414NIGMS NIH HHS GM065103NIGMS NIH HHS GM093528NIGMS NIH HHS R01 GM059414NIGMS NIH HHS T32 GM008732NIGMS NIH HHS T32 GM065103
6 · The paper itself

Abstract

Cdc13, the telomere end-binding protein from Saccharomyces cerevisiae, is a multidomain protein that specifically binds telomeric single-stranded DNA (ssDNA) with exquisitely high affinity to coordinate telomere maintenance. Recent structural and genetic data have led to the proposal that Cdc13 is the paralog of RPA70 within a telomere-specific RPA complex. Our understanding of Cdc13 structure and biochemistry has been largely restricted to studies of individual domains, precluding analysis of how each domain influences the activity of the others. To better facilitate a comparison to RPA70, we evaluated the ssDNA binding of full-length S. cerevisiae Cdc13 to its minimal substrate, Tel11. We found that, unlike RPA70 and the other known telomere end-binding proteins, the core Cdc13 ssDNA-binding activity is wholly contained within a single tight-binding oligosaccharide/oligonucleotide/oligopeptide binding (OB)-fold. Because two OB-folds are implicated in dimerization, we also evaluated the relationship between dimerization and ssDNA-binding activity and found that the two activities are independent. We also find that Cdc13 binding exhibits positive cooperativity that is independent of dimerization. This study reveals that, while Cdc13 and RPA70 share similar domain topologies, the corresponding domains have evolved different and specialized functions.

Indexed as

DNA, Single-StrandedProtein BindingProtein MultimerizationProtein Structure, TertiarySaccharomyces cerevisiae ProteinsTelomereTelomere-Binding ProteinsCdc13 protein, S cerevisiaeDNA, Single-StrandedSaccharomyces cerevisiae ProteinsTelomere-Binding Proteins

Identifiers

PMID24057216
PMCPMC3874162
OpenAlexW2121350840

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.