Evidence map›Paper›PMID 19115013›Full record

ArticlePloS one2008

Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I.

Robert Reiner, Natalie Krasnov-Yoeli, Yana Dehtiar, Nayef Jarrous

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  3. Human RNase P exhibits and controls distinct ribonucleolytic activities required for ordered maturation of tRNA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Article
  6. Article
  7. The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021
    Review
  8. Article
  9. The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021
    Review
  10. Article
  11. A mutation in POLR3E impairs antiviral immune response and RNA polymerase III.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

4 authors at 1 institution in 1 country.

Robert ReinerDepartment of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Natalie Krasnov-Yoeli
Yana Dehtiar
Nayef Jarrous
Hebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHuman RNase P has been initially described as a tRNA processing enzyme, consisting of H1 RNA and at least ten distinct protein subunits. Recent findings, however, indicate that this catalytic ribonucleoprotein is also required for transcription of small noncoding RNA genes by RNA polymerase III (Pol III). Notably, subunits of human RNase P are localized in the nucleolus, thus raising the possibility that this ribonucleoprotein complex is implicated in transcription of rRNA genes by Pol I. METHODOLOGY/PRINCIPAL

findingsBy using biochemical and reverse genetic means we show here that human RNase P is required for efficient transcription of rDNA by Pol I. Thus, inactivation of RNase P by targeting its protein subunits for destruction by RNA interference or its H1 RNA moiety for specific cleavage causes marked reduction in transcription of rDNA by Pol I. However, RNase P restores Pol I transcription in a defined reconstitution system. Nuclear run on assays reveal that inactivation of RNase P reduces the level of nascent transcription by Pol I, and more considerably that of Pol III. Moreover, RNase P copurifies and associates with components of Pol I and its transcription factors and binds to chromatin of the promoter and coding region of rDNA. Strikingly, RNase P detaches from transcriptionally inactive rDNA in mitosis and reassociates with it at G1 phase through a dynamic and stepwise assembly process that is correlated with renewal of transcription. CONCLUSIONS/SIGNIFICANCE: Our findings reveal that RNase P activates transcription of rDNA by Pol I through a novel assembly process and that this catalytic ribonucleoprotein determines the transcription output of Pol I and Pol III, two functionally coordinated transcription machineries.

Indexed as

Transcription, GeneticCell CycleCell NucleolusChromatinDNA, RibosomalHeLa CellsHumansPromoter Regions, GeneticProtein SubunitsRibonuclease PRibonucleoproteinsRNA Polymerase IRNA Polymerase IIITranscription FactorsChromatinDNA, RibosomalProtein SubunitsRibonuclease PRibonucleoproteinsRNA Polymerase IRNA Polymerase IIITranscription Factors

Identifiers

PMID19115013
PMCPMC2605565
OpenAlexW2002678747

What OpenQuestion holds

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LicenceCC BY
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.