Evidence map›Paper›PMID 11080168›Full record

ArticleThe EMBO journal2000

Euplotes telomerase contains an La motif protein produced by apparent translational frameshifting.

S Aigner, J Lingner, K J Goodrich, C A Grosshans, A Shevchenko, M Mann, T R Cech

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.4field-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

53 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Nontriplet feature of genetic code inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Structure ofRNA biology · 2021
    Article
  11. Review
  12. Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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

7 authors at 1 institution in 1 country.

S AignerDepartment of Chemistry and Biochemistry and Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309-0215, USA.
J Lingner
K J Goodrich
C A Grosshans
A Shevchenko
M Mann
T R Cech
Howard Hughes Medical Institute · US

Funding

Telomerase and Telomeres: Structure, Function/RegulationR01GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS ROBERT · 1985 to 2009
$2.6M
STUDIES OF NUCLEIC ACID STRUCTURE AND REACTIVITYR37GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS R · 1988 to 1997
–
NIGMS NIH HHS GM28039NIGMS NIH HHS R01 GM028039
6 · The paper itself

Abstract

Telomerase is the ribonucleoprotein enzyme responsible for the replication of chromosome ends in most eukaryotes. In the ciliate Euplotes aediculatus, the protein p43 biochemically co-purifies with active telomerase and appears to be stoichiometric with both the RNA and the catalytic protein subunit of this telomerase complex. Here we describe cloning of the gene for p43 and present evidence that it is an authentic component of the telomerase holoenzyme. Comparison of the nucleotide sequence of the cloned gene with peptide sequences of the protein suggests that production of full-length p43 relies on a programmed ribosomal frameshift, an extremely rare translational mechanism. Anti-p43 antibodies immunodeplete telomerase RNA and telomerase activity from E.aediculatus nuclear extracts, indicating that the vast majority of mature telomerase complexes in the cell are associated with p43. The sequence of p43 reveals similarity to the La autoantigen, an RNA-binding protein involved in maturation of RNA polymerase III transcripts, and recombinant p43 binds telomerase RNA in vitro. By analogy to other La proteins, p43 may function in chaperoning the assembly and/or facilitating nuclear retention of telomerase.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAutoantigensBase SequenceCloning, MolecularEscherichia coliEuplotesFrameshifting, RibosomalGenes, ProtozoanMolecular Sequence DataProtein BiosynthesisProtein Processing, Post-TranslationalRecombinant ProteinsRibonucleoproteinsRNA, MessengerAutoantigensRecombinant ProteinsRibonucleoproteinsRNA, MessengerRNA, ProtozoanSS-B AntigenTelomerase

Identifiers

PMID11080168
PMCPMC305813
OpenAlexW2157598684

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.