Evidence map›Paper›PMID 10444065›Full record

ArticleThe Journal of cell biology1999

Localization in the nucleolus and coiled bodies of protein subunits of the ribonucleoprotein ribonuclease P.

N Jarrous, J S Wolenski, D Wesolowski, C Lee, S Altman

Abstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
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

52 citing papers in PubMed.

  1. RNase MRP subunit composition and role in 40S ribosome biogenesis.Nature structural & molecular biology · 2026
    Article
  2. Review
  3. Review
  4. Review
  5. The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021
    Review
  6. Review
  7. Article
  8. The Nucleolus: In Genome Maintenance and Repair.International journal of molecular sciences · 2017
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. tRNA biology charges to the front.Genes & development · 2010
    Review
  14. Ribosomal protein L7Ae is a subunit of archaeal RNase P.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  15. Article
  16. Article
  17. The role of the plant nucleolus in pre-mRNA processing.Current topics in microbiology and immunology · 2008
    Review
  18. Review
  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

5 authors.

N JarrousDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA.
J S Wolenski
D Wesolowski
C Lee
S Altman

Funding

TRNA: STUDIES OF PRECURSORS, MUTANTS AND FUNCTIONSR01GM019422 · NIGMS · YALE UNIVERSITY · PI ALTMAN, SIDNEY · 1985 to 2003
$2.4M
TRNA: STUDIES OF PRECURSORS, MUTANTS, AND FUNCTIONR37GM019422 · NIGMS · YALE UNIVERSITY · PI ALTMAN, SIDNEY · 1989 to 1999
–
NIGMS NIH HHS GM-19422NIGMS NIH HHS R01 GM019422NIGMS NIH HHS R37 GM019422
6 · The paper itself

Abstract

The precise location of the tRNA processing ribonucleoprotein ribonuclease P (RNase P) and the mechanism of its intranuclear distribution have not been completely delineated. We show that three protein subunits of human RNase P (Rpp), Rpp14, Rpp29 and Rpp38, are found in the nucleolus and that each can localize a reporter protein to nucleoli of cells in tissue culture. In contrast to Rpp38, which is uniformly distributed in nucleoli, Rpp14 and Rpp29 are confined to the dense fibrillar component. Rpp29 and Rpp38 possess functional, yet distinct domains required for subnucleolar localization. The subunit Rpp14 lacks such a domain and appears to be dependent on a piggyback process to reach the nucleolus. Biochemical analysis suggests that catalytically active RNase P exists in the nucleolus. We also provide evidence that Rpp29 and Rpp38 reside in coiled bodies, organelles that are implicated in the biogenesis of several other small nuclear ribonucleoproteins required for processing of precursor mRNA. Because some protein subunits of RNase P are shared by the ribosomal RNA processing ribonucleoprotein RNase MRP, these two evolutionary related holoenzymes may share common intranuclear localization and assembly pathways to coordinate the processing of tRNA and rRNA precursors.

Indexed as

Amino Acid SequenceAnimalsAutoantigensBiological TransportCatalysisCell LineCell NucleolusEndoribonucleasesHoloenzymesHumansMiceMolecular Sequence DataMolecular WeightOrganellesProtein Sorting SignalsRibonuclease PAutoantigensEndoribonucleasesHoloenzymesProtein Sorting SignalsRibonuclease PRibonucleoproteinsRNA, CatalyticRNA PrecursorsRNA, Transfer, SerRPP14 protein, humanRPP38 protein, human

Identifiers

PMID10444065
PMCPMC2150555

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.