Evidence map›Paper›PMID 23300477›Full record

ArticlePLoS genetics2013

The telomere capping complex CST has an unusual stoichiometry, makes multipartite interaction with G-Tails, and unfolds higher-order G-tail structures.

Neal F Lue, Ruobo Zhou, Lidia Chico, Ninghui Mao, Olga Steinberg-Neifach, Taekjip Ha

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Telomere Replication: Solving Multiple End Replication Problems.Frontiers in cell and developmental biology · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Emerging roles of CST in maintaining genome stability and human disease.Frontiers in bioscience (Landmark edition) · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017
    Review
  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

6 authors at 4 institutions in 1 country.

Neal F LueDepartment of Microbiology and Immunology, W. R. Hearst Microbiology Research Center, Weill Medical College of Cornell University, New York, New York, USA. nflue@med.cornell.edu
Ruobo Zhou
Lidia Chico
Ninghui Mao
Olga Steinberg-Neifach
Taekjip Ha
Hearst (United States) · USUniversity of Illinois Urbana-Champaign · USCornell University · USHostos Community College · US

Funding

Single Molecule Study of Helicase MechanismsR01GM065367 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HA, TAEKJIP · 2002 to 2014
$3.6M
ANALYSIS OF TELOMERASE REVERSE TRANSCRIPTASER01GM062631 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LUE, NEAL F · 2001 to 2010
$3.0M
Howard Hughes Medical InstituteNIGMS NIH HHS GM062631NIGMS NIH HHS GM065367NIGMS NIH HHS R01 GM062631NIGMS NIH HHS R01 GM065367
6 · The paper itself

Abstract

The telomere-ending binding protein complex CST (Cdc13-Stn1-Ten1) mediates critical functions in both telomere protection and replication. We devised a co-expression and affinity purification strategy for isolating large quantities of the complete Candida glabrata CST complex. The complex was found to exhibit a 2∶4∶2 or 2∶6∶2 stoichiometry as judged by the ratio of the subunits and the native size of the complex. Stn1, but not Ten1 alone, can directly and stably interact with Cdc13. In gel mobility shift assays, both Cdc13 and CST manifested high-affinity and sequence-specific binding to the cognate telomeric repeats. Single molecule FRET-based analysis indicates that Cdc13 and CST can bind and unfold higher order G-tail structures. The protein and the complex can also interact with non-telomeric DNA in the absence of high-affinity target sites. Comparison of the DNA-protein complexes formed by Cdc13 and CST suggests that the latter can occupy a longer DNA target site and that Stn1 and Ten1 may contact DNA directly in the full CST-DNA assembly. Both Stn1 and Ten1 can be cross-linked to photo-reactive telomeric DNA. Mutating residues on the putative DNA-binding surface of Candida albicans Stn1 OB fold domain caused a reduction in its crosslinking efficiency in vitro and engendered long and heterogeneous telomeres in vivo, indicating that the DNA-binding activity of Stn1 is required for telomere protection. Our data provide insights on the assembly and mechanisms of CST, and our robust reconstitution system will facilitate future biochemical analysis of this important complex.

Indexed as

Cell Cycle ProteinsSaccharomyces cerevisiae ProteinsCandida albicansCandida glabrataChromosomal Proteins, Non-HistoneDNA ReplicationFungal ProteinsProtein BindingProtein FoldingProtein Structure, TertiarySaccharomyces cerevisiaeTelomereTelomere-Binding ProteinsCdc13 protein, S cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistoneFungal ProteinsSaccharomyces cerevisiae ProteinsStn1 protein, S cerevisiaeTelomere-Binding ProteinsTEN1 protein, S cerevisiae

Identifiers

PMID23300477
PMCPMC3536697
OpenAlexW2125469057

What OpenQuestion holds

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LicenceCC BY
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.