Evidence map›Paper›PMID 22025677›Full record

ArticleMolecular and cellular biology2012

Analyses of Candida Cdc13 orthologues revealed a novel OB fold dimer arrangement, dimerization-assisted DNA binding, and substantial structural differences between Cdc13 and RPA70.

Eun Young Yu, Jia Sun, Ming Lei, Neal F Lue

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. Evolutionary relationship between yeast telomeric protein Cdc13 and Pot1.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Article
  2. Review
  3. Article
  4. Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021
    Review
  5. Article
  6. Emerging roles of CST in maintaining genome stability and human disease.Frontiers in bioscience (Landmark edition) · 2018
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Structure and function of the telomeric CST complex.Computational and structural biotechnology journal · 2016
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  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

4 authors at 3 institutions in 1 country.

Eun Young YuDepartment of Microbiology & Immunology, WR Hearst Microbiology Research Center, Weill Medical College of Cornell University, New York, New York, USA.
Jia Sun
Ming Lei
Neal F Lue
University of Michigan–Ann Arbor · USCornell University · USHearst (United States) · US

Funding

Structure of the Telomere Shelterin ComplexR01GM083015 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LEI, MING · 2008 to 2012
$1.2M
Telomerase function and regulation in a new model systemR01GM069507 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LUE, NEAL F · 2004 to 2007
$1.2M
Howard Hughes Medical InstituteNCI NIH HHS Y1-CO-1020NIGMS NIH HHS GM069507NIGMS NIH HHS GM083015-01NIGMS NIH HHS R01 GM069507NIGMS NIH HHS R01 GM083015NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The budding yeast Cdc13-Stn1-Ten1 complex is crucial for telomere protection and has been proposed to resemble the RPA complex structurally and functionally. The Cdc13 homologues in Candida species are unusually small and lack two conserved domains previously implicated in telomere regulation, thus raising interesting questions concerning the mechanisms and evolution of these proteins. In this report, we show that the unusually small Cdc13 homologue in Candida albicans is indeed a regulator of telomere lengths and that it associates with telomere DNA in vivo. We demonstrated high-affinity telomere DNA binding by C. tropicalis Cdc13 (CtCdc13) and found that dimerization of this protein through its OB4 domain is important for high-affinity DNA binding. Interestingly, CtCdc13-DNA complex formation appears to involve primarily recognition of multiple copies of a six-nucleotide element (GGATGT) that is shared by many Candida telomere repeats. We also determined the crystal structure of the OB4 domain of C. glabrata Cdc13, which revealed a novel mechanism of OB fold dimerization. The structure also exhibits marked differences to the C-terminal OB fold of RPA70, thus arguing against a close evolutionary kinship between these two proteins. Our findings provide new insights on the mechanisms and evolution of a critical telomere end binding protein.

Indexed as

Base SequenceBinding SitesCandidaCandida albicansCandida glabrataCandida tropicalisDNA, FungalFungal ProteinsModels, MolecularMutationProtein BindingProtein MultimerizationProtein Structure, TertiaryTelomereTelomere-Binding ProteinsDNA, FungalFungal ProteinsTelomere-Binding Proteins

Identifiers

PMID22025677
PMCPMC3255709
OpenAlexW2146334001

What OpenQuestion holds

Textmetadata
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.