Evidence map›Paper›PMID 32358529›Full record

ArticleNature communications2020

Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP.

P Daniela Garcia, Robert W Leach, Gable M Wadsworth, Krishna Choudhary, Hua Li, Sharon Aviran, Harold D Kim, Virginia A Zakian

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  8. Article
  9. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

P Daniela GarciaDepartment of Molecular Biology, Princeton University, Princeton, NJ, 08544, USA.
Robert W LeachBioinformatics Group, Genomics Core Facility, Carl Icahn Laboratory, Princeton University, Princeton, New Jersey, 08544, USA.ORCID http://orcid.org/0000-0001-5153-7754
Gable M WadsworthSchool of Physics, Georgia Institute of Technology, Atlanta, Georgia, 30332, USA.
Krishna ChoudharyDepartment of Biomedical Engineering and Genome Center, University of California, Davis, California, 95616, USA.
Hua LiDepartment of Biomedical Engineering and Genome Center, University of California, Davis, California, 95616, USA.
Sharon AviranDepartment of Biomedical Engineering and Genome Center, University of California, Davis, California, 95616, USA.ORCID http://orcid.org/0000-0003-1872-9820
Harold D KimSchool of Physics, Georgia Institute of Technology, Atlanta, Georgia, 30332, USA.ORCID http://orcid.org/0000-0003-0878-2169
Virginia A ZakianDepartment of Molecular Biology, Princeton University, Princeton, NJ, 08544, USA. vzakian@princeton.edu.
Princeton University · USGeorgia Institute of Technology · USUniversity of California, Davis · USGladstone Institutes · US

Funding

Telomere maintenance and replication fork progression in yeast and human cellsR35GM118279 · NIGMS · PRINCETON UNIVERSITY · PI ZAKIAN, VIRGINIA A. · 2016 to 2020
$4.5M
Investigation of energetics of sharp DNA bendingR01GM112882 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI KIM, HAROLD D · 2015 to 2023
$2.6M
NIGMS NIH HHS R01 GM112882NIGMS NIH HHS R35 GM118279
6 · The paper itself

Abstract

RNase P and MRP are highly conserved, multi-protein/RNA complexes with essential roles in processing ribosomal and tRNAs. Three proteins found in both complexes, Pop1, Pop6, and Pop7 are also telomerase-associated. Here, we determine how temperature sensitive POP1 and POP6 alleles affect yeast telomerase. At permissive temperatures, mutant Pop1/6 have little or no effect on cell growth, global protein levels, the abundance of Est1 and Est2 (telomerase proteins), and the processing of TLC1 (telomerase RNA). However, in pop mutants, TLC1 is more abundant, telomeres are short, and TLC1 accumulates in the cytoplasm. Although Est1/2 binding to TLC1 occurs at normal levels, Est1 (and hence Est3) binding is highly unstable. We propose that Pop-mediated stabilization of Est1 binding to TLC1 is a pre-requisite for formation and nuclear localization of the telomerase holoenzyme. Furthermore, Pop proteins affect TLC1 and the RNA subunits of RNase P/MRP in very different ways.

Indexed as

Cell NucleusDNA-Binding ProteinsMethylationProtein BindingRibonuclease PRibonucleoproteinsRNARNA 3' End ProcessingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomeraseTelomereDNA-Binding ProteinsEST1 protein, S cerevisiaeEST3 protein, S cerevisiaePOP1 protein, S cerevisiaePOP6 protein, S cerevisiaePOP7 protein, S cerevisiaeRibonuclease PRibonucleoproteinsRNASaccharomyces cerevisiae ProteinsTelomerasetelomerase RNAYKU70 protein, S cerevisiae

Identifiers

PMID32358529
PMCPMC7195438
OpenAlexW3021103109

What OpenQuestion holds

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Registered trials

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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.