Evidence map›Paper›PMID 21685334›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA.

Wei-Feng Yen, Lidia Chico, Ming Lei, Neal F Lue

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013
    Review
  11. A popular engagement at the ends.Nature structural & molecular biology · 2013
    Article
  12. Article
  13. Review
  14. Article
  15. Telomerase and retrotransposons: reverse transcriptases that shaped genomes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Structural anatomy of telomere OB proteins.Critical reviews in biochemistry and molecular biology · 2011
    Review
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.

Wei-Feng YenDepartment of Microbiology and Immunology, W. R. Hearst Microbiology Research Center, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.
Lidia Chico
Ming Lei
Neal F Lue
Hearst (United States) · USCornell University · USUniversity of Michigan–Ann Arbor · US

Funding

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 InstituteNIGMS NIH HHS GM-069507NIGMS NIH HHS R01 GM069507
6 · The paper itself

Abstract

The yeast telomerase regulatory protein Est3 is required for telomere maintenance in vivo, and shares intriguing structural and functional similarities with the mammalian telomeric protein TPP1. Here we report our physical and functional characterizations of Est3 homologues from Candida parapsilosis and Lodderomyces elongisporus, which bear unique N- and C-terminal tails in addition to a conserved central OB fold. We show that these Est3 homologues form stable complexes with the TEN domain of telomerase reverse transcriptase. Efficient complex formation requires both the N- and C-terminal tails, as well as conserved OB fold residues of Est3. Other Est3 homologues devoid of the tails failed to interact strongly with the cognate TEN domains. Remarkably, the C. parapsilosis Est3 alone exhibits no appreciable DNA-binding activity, but can be crosslinked to telomeric DNA in the presence of the TEN domain. A conserved basic residue on the putative DNA-binding surface of CpEst3 is required for efficient crosslinking. Mutating the equivalent residue in Candida albicans Est3 caused telomere attrition. We propose that interaction with the TEN domain unmasks a functionally important nucleic acid-binding activity in Est3. Our findings provide insights on the mechanisms and evolution of a widely conserved and functionally critical telomeric/telomerase component.

Indexed as

AllelesBacterial ProteinsCandidaCandida albicansCross-Linking ReagentsDNADNA-Binding ProteinsModels, GeneticMolecular ConformationMutationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityTelomeraseTelomereBacterial ProteinsCross-Linking ReagentsDNADNA-Binding ProteinsEST3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTelomerase

Identifiers

PMID21685334
PMCPMC3251127
OpenAlexW2022824390

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.