Evidence map›Paper›PMID 22850424›Full record

ArticleRNA (New York, N.Y.)2012

Stiffened yeast telomerase RNA supports RNP function in vitro and in vivo.

Kevin J Lebo, David C Zappulla

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Inverse-folding design of yeast telomerase RNA increases activitybioRxiv : the preprint server for biology · 2023
    Article
  3. Review
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  12. Article
  13. Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013
    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

2 authors at 1 institution in 1 country.

Kevin J LeboDepartment of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.
David C Zappulla
Johns Hopkins University · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
Investigating Telomerase Mechanism by Exploring the RNAR00GM080400 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ZAPPULLA, DAVID CLIFFORD · 2008 to 2010
$745k
Investigating Telomerase Mechanism by Exploring the RNAK99GM080400 · NIGMS · UNIVERSITY OF COLORADO · PI ZAPPULLA, DAVID CLIFFORD · 2007 to 2008
$106k
NIGMS NIH HHS 2T32 GM007231NIGMS NIH HHS K99 GM080400NIGMS NIH HHS R00 GM080400NIGMS NIH HHS R00 GM80400NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

The 1157-nt Saccharomyces cerevisiae telomerase RNA, TLC1, in addition to providing a 16-nt template region for reverse transcription, has been proposed to act as a scaffold for protein subunits. Although accessory subunits of the telomerase ribonucleoprotein (RNP) complex function even when their binding sites are relocated on the yeast telomerase RNA, the physical nature of the RNA scaffold has not been directly analyzed. Here we explore the structure-function organization of the yeast telomerase RNP by extensively stiffening the three long arms of TLC1, which connect essential and important accessory protein subunits Ku, Est1, and Sm(7), to its central catalytic hub. This 956-nt triple-stiff-arm TLC1 (TSA-T) reconstitutes active telomerase with TERT (Est2) in vitro. Furthermore, TSA-T functions in vivo, even maintaining longer telomeres than TLC1 on a per RNA basis. We also tested functional contributions of each stiffened arm within TSA-T and found that the stiffened Est1 and Ku arms contribute to telomere lengthening, while stiffening the terminal arm reduces telomere length and telomerase RNA abundance. The fact that yeast telomerase tolerates significant stiffening of its RNA subunit in vivo advances our understanding of the architectural and functional organization of this RNP and, more broadly, our conception of the world of lncRNPs.

Indexed as

Base SequenceDNA-Binding ProteinsModels, BiologicalNucleic Acid ConformationProtein BindingRibonucleoproteinsRNASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomeraseTelomereDNA-Binding ProteinsEST1 protein, S cerevisiaehigh affinity DNA-binding factor, S cerevisiaeRibonucleoproteinsRNASaccharomyces cerevisiae ProteinsTelomerasetelomerase RNA

Identifiers

PMID22850424
PMCPMC3425781
OpenAlexW2112675198

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.