Evidence map›Paper›PMID 11274393›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

M Gautschi, H Lilie, U Fünfschilling, A Mun, S Ross, T Lithgow, P Rücknagel, S Rospert

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

114 citing papers in PubMed, 233 citations in OpenAlex.

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  8. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Article
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  14. Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Anti-Prion Systems inViruses · 2022
    Review

54 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

8 authors at 1 institution in 1 country.

M GautschiEnzymology of Protein Folding, Max Planck Research Laboratory, Weinbergweg 22, D-06120 Halle/Saale, Germany.
H Lilie
U Fünfschilling
A Mun
S Ross
T Lithgow
P Rücknagel
S Rospert
Max Planck Research Unit for Enzymology of Protein Folding · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast cytosol contains multiple homologs of the DnaK and DnaJ chaperone family. Our current understanding of which homologs functionally interact is incomplete. Zuotin is a DnaJ homolog bound to the yeast ribosome. We have now identified the DnaK homolog Ssz1p/Pdr13p as zuotin's partner chaperone. Zuotin and Ssz1p form a ribosome-associated complex (RAC) that is bound to the ribosome via the zuotin subunit. RAC is unique among the eukaryotic DnaK-DnaJ systems, as the 1:1 complex is stable, even in the presence of ATP or ADP. In vitro, RAC stimulates the translocation of a ribosome-bound mitochondrial precursor protein into mitochondria, providing evidence for its chaperone-like effect on nascent chains. In agreement with the existence of a functional complex, deletion of each RAC subunit resulted in a similar phenotype in vivo. However, overexpression of zuotin partly rescued the growth defect of the Delta ssz1 strain, whereas overexpression of Ssz1p did not affect the Delta zuo1 strain, suggesting a pivotal function for the DnaJ homolog.

Indexed as

Escherichia coli ProteinsSaccharomyces cerevisiae ProteinsCytosolDimerizationDNA-Binding ProteinsFungal ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMitochondriaMolecular ChaperonesSaccharomyces cerevisiaeDNA-Binding ProteinsDnaJ protein, E colidnaK protein, E coliEscherichia coli ProteinsFungal ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsSSZ1 protein, S cerevisiaeZUO1 protein, S cerevisiae

Identifiers

PMID11274393
PMCPMC31126
OpenAlexW1981873223

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.