Evidence map›Paper›PMID 15456889›Full record

ArticleMolecular and cellular biology2004

The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae.

Magdalena Rakwalska, Sabine Rospert

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

57 citing papers in PubMed, 95 citations in OpenAlex.

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  11. Paromomycin ReducesMicroorganisms · 2022
    Article
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  17. Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Chaperone Interactions at the Ribosome.Cold Spring Harbor perspectives in biology · 2019
    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

2 authors at 1 institution in 1 country.

Magdalena RakwalskaInstitut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany.
Sabine Rospert
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chaperone homologs RAC (ribosome-associated complex) and Ssb1/2p are anchored to ribosomes; Ssb1/2p directly interacts with nascent polypeptides. The absence of RAC or Ssb1/2p results in a similar set of phenotypes, including hypersensitivity against the aminoglycoside paromomycin, which binds to the small ribosomal subunit and compromises the fidelity of translation. In order to understand this phenomenon we measured the frequency of translation termination and misincorporation in vivo and in vitro with a novel reporter system. Translational fidelity was impaired in the absence of functional RAC or Ssb1/2p, and the effect was further enhanced by paromomycin. The mutant strains suffered primarily from a defect in translation termination, while misincorporation was compromised to a lesser extent. Consistently, a low level of soluble translation termination factor Sup35p enhanced growth defects in the mutant strains. Based on the combined data we conclude that RAC and Ssb1/2p are crucial in maintaining translational fidelity beyond their postulated role as chaperones for nascent polypeptides.

Indexed as

Protein BiosynthesisAdenosine TriphosphatasesAmino Acid SequenceAnti-Bacterial AgentsBase SequenceDNA-Binding ProteinsGene Expression Regulation, FungalGenes, ReporterHSP70 Heat-Shock ProteinsMacromolecular SubstancesMolecular ChaperonesMolecular Sequence DataParomomycinPeptide Termination FactorsPoint MutationProtein BindingAdenosine TriphosphatasesAnti-Bacterial AgentsDNA-Binding ProteinsHSP70 Heat-Shock ProteinsMacromolecular SubstancesMolecular ChaperonesParomomycinPeptide Termination FactorsSaccharomyces cerevisiae ProteinsSSB1 protein, S cerevisiaeSSB2 protein, S cerevisiae

Identifiers

PMID15456889
PMCPMC517888
OpenAlexW2104504238

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.