Evidence map›Paper›PMID 27156450›Full record

ArticleCell2016

Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP.

Bruno Lemieux, Nancy Laterreur, Anna Perederina, Jean-François Noël, Marie-Line Dubois, Andrey S Krasilnikov, Raymund J Wellinger

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

61 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. bioRxiv : the preprint server for biology · 2026
    Article
  5. Molecular and cellular biology · 2026
    Article
  6. Article
  7. Ectopic overexpression ofMicrobiology spectrum · 2025
    Article
  8. Article
  9. Review
  10. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  17. Review
  18. Review
  19. Inverse-folding design of yeast telomerase RNA increases activitybioRxiv : the preprint server for biology · 2023
    Article
  20. Review

1 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Bruno LemieuxDepartment of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
Nancy LaterreurDepartment of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
Anna PerederinaDepartment of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Jean-François NoëlDepartment of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
Marie-Line DuboisDepartment of Anatomy and Cellular Biology,Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
Andrey S KrasilnikovDepartment of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Raymund J WellingerDepartment of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada. Electronic address: raymund.wellinger@usherbrooke.ca.
Université de Sherbrooke · CAPennsylvania State University · US

Funding

Proteins in RNA-Based EnzymesR01GM085149 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI KRASILNIKOV, ANDREY S. · 2008 to 2017
$2.9M
NIGMS NIH HHS R01 GM085149
6 · The paper itself

Abstract

Telomerase is the ribonucleoprotein enzyme that replenishes telomeric DNA and maintains genome integrity. Minimally, telomerase activity requires a templating RNA and a catalytic protein. Additional proteins are required for activity on telomeres in vivo. Here, we report that the Pop1, Pop6, and Pop7 proteins, known components of RNase P and RNase MRP, bind to yeast telomerase RNA and are essential constituents of the telomerase holoenzyme. Pop1/Pop6/Pop7 binding is specific and involves an RNA domain highly similar to a protein-binding domain in the RNAs of RNase P/MRP. The results also show that Pop1/Pop6/Pop7 function to maintain the essential components Est1 and Est2 on the RNA in vivo. Consistently, addition of Pop1 allows for telomerase activity reconstitution with wild-type telomerase RNA in vitro. Thus, the same chaperoning module has allowed the evolution of functionally and, remarkably, structurally distinct RNPs, telomerase, and RNases P/MRP from unrelated progenitor RNAs.

Indexed as

EndoribonucleasesImmunoprecipitationMass SpectrometryModels, MolecularRibonuclease PRibonucleoproteinsRNA, FungalSaccharomyces cerevisiae ProteinsSaccharomycetalesTelomeraseEndoribonucleasesEST1 protein, S cerevisiaeEST2 protein, S cerevisiaemitochondrial RNA-processing endoribonucleasePOP1 protein, S cerevisiaePOP6 protein, S cerevisiaePOP7 protein, S cerevisiaeRibonuclease PRibonucleoproteinsRNA, FungalSaccharomyces cerevisiae ProteinsTelomerase

Identifiers

PMID27156450
PMCPMC4874874
OpenAlexW2346481077

What OpenQuestion holds

Textmetadata
LicenceTDM
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.