Evidence map›Paper›PMID 20106956›Full record

ArticleRNA (New York, N.Y.)2010

Ciliate telomerase RNA loop IV nucleotides promote hierarchical RNP assembly and holoenzyme stability.

Aaron R Robart, Catherine M O'Connor, Kathleen Collins

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018
    Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. RNA-protein binding interface in the telomerase ribonucleoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Article
  14. Telomerase: an RNP enzyme synthesizes DNA.Cold Spring Harbor perspectives in biology · 2011
    Review
  15. 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

3 authors at 1 institution in 1 country.

Aaron R RobartDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720-3200, USA.
Catherine M O'Connor
Kathleen Collins
University of California, Berkeley · US

Funding

STRUCTURE AND FUNCTION OF TELOMERASER01GM054198 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 1996 to 2018
$5.4M
NIGMS NIH HHS GM054198NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

Telomerase adds simple-sequence repeats to chromosome 3' ends to compensate for the loss of repeats with each round of genome replication. To accomplish this de novo DNA synthesis, telomerase uses a template within its integral RNA component. In addition to providing the template, the telomerase RNA subunit (TER) also harbors nontemplate motifs that contribute to the specialized telomerase catalytic cycle of reiterative repeat synthesis. Most nontemplate TER motifs function through linkage with the template, but in ciliate and vertebrate telomerases, a stem-loop motif binds telomerase reverse transcriptase (TERT) and reconstitutes full activity of the minimal recombinant TERT+TER RNP, even when physically separated from the template. Here, we resolve the functional requirements for this motif of ciliate TER in physiological RNP context using the Tetrahymena thermophila p65-TER-TERT core RNP reconstituted in vitro and the holoenzyme reconstituted in vivo. Contrary to expectation based on assays of the minimal recombinant RNP, we find that none of a panel of individual loop IV nucleotide substitutions impacts the profile of telomerase product synthesis when reconstituted as physiological core RNP or holoenzyme RNP. However, loop IV nucleotide substitutions do variably reduce assembly of TERT with the p65-TER complex in vitro and reduce the accumulation and stability of telomerase RNP in endogenous holoenzyme context. Our results point to a unifying model of a conformational activation role for this TER motif in the telomerase RNP enzyme.

Indexed as

Enzyme StabilityNucleic Acid ConformationRNARNA, ProtozoanTelomeraseTetrahymena thermophilaRNARNA, ProtozoanTelomerasetelomerase RNA

Identifiers

PMID20106956
PMCPMC2822921
OpenAlexW2157638309

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.