Evidence map›Paper›PMID 15899850›Full record

ArticleMolecular and cellular biology2005

Biological and biochemical functions of RNA in the tetrahymena telomerase holoenzyme.

Doreen D Cunningham, Kathleen Collins

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Progress in structural studies of telomerase.Current opinion in structural biology · 2014
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Single-stranded DNA repeat synthesis by telomerase.Current opinion in chemical biology · 2011
    Review
  16. Telomerase: an RNP enzyme synthesizes DNA.Cold Spring Harbor perspectives in biology · 2011
    Review
  17. Article
  18. Article
  19. Article
  20. High-resolution physical and functional mapping of the template adjacent DNA binding site in catalytically active telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

2 authors at 1 institution in 1 country.

Doreen D CunninghamDepartment of Molecular and Cell Biology, 16 Barker Hall, University of California, Berkeley, CA 94720-3204, USA.
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 GM54198NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

Telomerase extends chromosome ends by the synthesis of tandem simple-sequence repeats. Studies of minimal recombinant telomerase ribonucleoprotein (RNP) reconstituted in vitro have revealed sequences within the telomerase RNA subunit (TER) that are required to establish its internal template and other unique features of enzyme activity. Here we test the significance of these motifs following TER assembly into telomerase holoenzyme in vivo. We established a method for stable expression of epitope-tagged TER and TER variants in place of wild-type Tetrahymena TER. We found that sequence substitutions in nontemplate regions of TER altered telomere length maintenance in vivo, with an increase or decrease in the set point for telomere length homeostasis. We also characterized the in vitro activity of the telomerase holoenzymes reconstituted with TER variants, following RNA-based RNP affinity purification from cell extracts. We found that nontemplate sequence substitutions imposed specific defects in the fidelity and processivity of template use. These findings demonstrate nontemplate functions of TER that are critical for the telomerase holoenzyme catalytic cycle and for proper telomere length maintenance in vivo.

Indexed as

AnimalsCatalysisHoloenzymesMutationNuclear ProteinsNucleic Acid ConformationPhosphoproteinsProtozoan ProteinsRecombinant ProteinsRibonucleoproteinsRNATelomeraseTemplates, GeneticTetrahymena thermophilaHoloenzymesNuclear ProteinsPdd1 protein, TetrahymenaPhosphoproteinsProtozoan ProteinsRecombinant ProteinsRibonucleoproteinsRNATelomerasetelomerase RNA

Identifiers

PMID15899850
PMCPMC1140614
OpenAlexW2151745111

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.