Evidence map›Paper›PMID 21659533›Full record

ArticleThe Journal of biological chemistry2011

Stimulation of yeast telomerase activity by the ever shorter telomere 3 (Est3) subunit is dependent on direct interaction with the catalytic protein Est2.

Jennell M Talley, Diane C DeZwaan, Leslie D Maness, Brian C Freeman, Katherine L Friedman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

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  18. Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013
    Review
  19. A popular engagement at the ends.Nature structural & molecular biology · 2013
    Article
  20. Cdc13 at a crossroads of telomerase action.Frontiers in oncology · 2013
    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 2 institutions in 1 country.

Jennell M TalleyDepartment of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235, USA.
Diane C DeZwaan
Leslie D Maness
Brian C Freeman
Katherine L Friedman
Vanderbilt University · USUniversity of Illinois Urbana-Champaign · US

Funding

INTERDISCIPLINARY CARDIOVASCULAR RESEARCH FELLOWSHIPT32HL007121 · NHLBI · UNIVERSITY OF IOWA · PI LONDON, BARRY · 1985 to 2020
$15.1M
TRAINING PROGRAM IN CELLULAR, BIOCHEMICAL, &MOLECULAR ST32GM008554 · NIGMS · VANDERBILT UNIVERSITY · PI PATTON, JAMES G. · 1995 to 2020
$7.4M
Cell Cycle Regulation of Yeast Telomerase Assembly and FunctionR01GM080393 · NIGMS · VANDERBILT UNIVERSITY · PI FRIEDMAN, KATHERINE LOUISE · 2008 to 2012
$1.5M
NHLBI NIH HHS T32 HL007121NIGMS NIH HHS GM080393NIGMS NIH HHS R01 GM080393NIGMS NIH HHS T32 GM008554NIGMS NIH HHS T32 GM08554
6 · The paper itself

Abstract

Telomerase is a multisubunit enzyme that maintains genome stability through its role in telomere replication. Although the Est3 protein is long recognized as an essential telomerase component, how it associates with and functions in the telomerase complex has remained enigmatic. Here we provide the first evidence of a direct interaction between Saccharomyces cerevisiae Est3p and the catalytic protein subunit (Est2p) by demonstrating that recombinant Est3p binds the purified telomerase essential N-terminal (TEN) domain of Est2p in vitro. Mutations in a small cluster of amino acids predicted to lie on the surface of Est3p disrupt this interaction with Est2p, reduce assembly of Est3p with telomerase in vivo, and cause telomere shortening and senescence. We also show that recombinant Est3p stimulates telomerase activity above basal levels in vitro in a manner dependent on the Est2p TEN domain interaction. Together, these results define a direct binding interaction between Est3p and Est2p and reconcile the effect of S. cerevisiae Est3p with previous experiments showing that Est3p homologs in related yeast species influence telomerase activity. Additionally, it contributes functional support to the idea that Est3p is structurally related to the mammalian shelterin protein, TPP1, which also influences telomerase activity through interaction with the Est2p homolog, TERT.

Indexed as

MutationProtein BindingProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomeraseEST2 protein, S cerevisiaeEST3 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsTelomerase

Identifiers

PMID21659533
PMCPMC3143607
OpenAlexW2092851073

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.