Evidence map›Paper›PMID 17242366›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis.

Alison E Meyer, Nai-Jung Hung, Peizhen Yang, Arlen W Johnson, Elizabeth A Craig

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

62 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
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  13. Article
  14. The Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Eukaryotic ribosome assembly, transport and quality control.Nature structural & molecular biology · 2017
    Review

2 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

5 authors at 2 institutions in 1 country.

Alison E MeyerDepartment of Biochemistry, 433 Babcock Drive, University of Wisconsin, Madison, WI 53706, USA.
Nai-Jung Hung
Peizhen Yang
Arlen W Johnson
Elizabeth A Craig
University of Wisconsin–Madison · USThe University of Texas at Austin · US

Funding

MRNA DEGRADATION AND TRANSLATION CONTROL IN YEASTR01GM053655 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI JOHNSON, ARLEN W · 1995 to 2017
$5.1M
REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER37GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1999 to 2008
$3.3M
REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER01GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1985 to 2012
$1.9M
NIGMS NIH HHS GM31107NIGMS NIH HHS GM53655NIGMS NIH HHS R01 GM031107NIGMS NIH HHS R01 GM053655NIGMS NIH HHS R37 GM031107
6 · The paper itself

Abstract

J-proteins and Hsp70 chaperones function together in diverse cellular processes. We identified a cytosolic J-protein, Jjj1, of Saccharomyces cerevisiae that is associated with 60S ribosomal particles. Unlike Zuo1, a 60S subunit-associated J-protein that is a component of the chaperone machinery that binds nascent polypeptide chains upon their exit from the ribosome, Jjj1 plays a role in ribosome biogenesis. Cells lacking Jjj1 have phenotypes very similar to those lacking Rei1, a ribosome biogenesis factor associated with pre-60S ribosomal particles in the cytosol. Jjj1 stimulated the ATPase activity of the general cytosolic Hsp70 Ssa, but not Ssb, Zuo1's ribosome-associated Hsp70 partner. Overexpression of Jjj1, which is normally approximately 40-fold less abundant than Zuo1, can partially rescue the phenotypes of cells lacking Zuo1 as well as cells lacking Ssb. Together, these results are consistent with the idea that Jjj1 normally functions with Ssa in a late, cytosolic step of the biogenesis of 60S ribosomal subunits. In addition, because of its ability to bind 60S subunits, we hypothesize that Jjj1, when overexpressed, is able to partially substitute for the Zuo1:Ssb chaperone machinery by recruiting Ssa to the ribosome, facilitating its interaction with nascent polypeptide chains.

Indexed as

Adenosine TriphosphatasesCytosolDimerizationDNA-Binding ProteinsGene Expression Regulation, FungalHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPhenotypeProtein BindingProtein Structure, TertiaryRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemperatureAdenosine TriphosphatasesDNA-Binding ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsJjj1 protein, S cerevisiaeMolecular ChaperonesREI1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSSA1 protein, S cerevisiaeSSB1 protein, S cerevisiaeZUO1 protein, S cerevisiae

Identifiers

PMID17242366
PMCPMC1785244
OpenAlexW2090227913

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.