Evidence map›Paper›PMID 24072706›Full record

ArticleThe Journal of biological chemistry2013

Interaction of nascent chains with the ribosomal tunnel proteins Rpl4, Rpl17, and Rpl39 of Saccharomyces cerevisiae.

Ying Zhang, Tina Wölfle, Sabine Rospert

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Engineering small peptide secretion inFrontiers in bioengineering and biotechnology · 2026
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  10. Ribosome heterogeneity and specialization in development.Wiley interdisciplinary reviews. RNA · 2021
    Review
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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

3 authors at 1 institution in 1 country.

Ying ZhangInstitute of Biochemistry and Molecular Biology, ZBMZ Centre for Biochemistry and Molecular Cell Research, University of Freiburg, Stefan-Meier-Strasse 17, D-79104 Freiburg, Germany; Centre for Biological Signalling Studies (BIOSS), University of Freiburg, D-79104 Freiburg, Germany.
Tina WölfleInstitute of Biochemistry and Molecular Biology, ZBMZ Centre for Biochemistry and Molecular Cell Research, University of Freiburg, Stefan-Meier-Strasse 17, D-79104 Freiburg, Germany.
Sabine RospertInstitute of Biochemistry and Molecular Biology, ZBMZ Centre for Biochemistry and Molecular Cell Research, University of Freiburg, Stefan-Meier-Strasse 17, D-79104 Freiburg, Germany; Centre for Biological Signalling Studies (BIOSS), University of Freiburg, D-79104 Freiburg, Germany. Electronic address: sabine.rospert@biochemie.uni-freiburg.de.
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As translation proceeds, nascent polypeptides pass through an exit tunnel that traverses the large ribosomal subunit. Three ribosomal proteins, termed Rpl4, Rpl17, and Rpl39 expose domains to the interior of the exit tunnel of eukaryotic ribosomes. Here we generated ribosome-bound nascent chains in a homologous yeast translation system to analyze contacts between the tunnel proteins and nascent chains. As model proteins we employed Dap2, which contains a hydrophobic signal anchor (SA) segment, and the chimera Dap2α, in which the SA was replaced with a hydrophilic segment, with the propensity to form an α-helix. Employing a newly developed FLAG exposure assay, we find that the nascent SA segment but not the hydrophilic segment adopted a stable, α-helical structure within the tunnel when the most C-terminal SA residue was separated by 14 residues from the peptidyl transferase center. Using UV cross-linking, antibodies specifically recognizing Rpl17 or Rpl39, and a His6-tagged version of Rpl4, we established that all three tunnel proteins of yeast contact the SA, whereas only Rpl4 and Rpl39 also contact the hydrophilic segment. Consistent with the localization of the tunnel exposed domains of Rpl17 and Rpl39, the SA was in contact with Rpl17 in the middle region and with Rpl39 in the exit region of the tunnel. In contrast, Rpl4 was in contact with nascent chain residues throughout the ribosomal tunnel.

Indexed as

Peptidyl TransferasesProtein BiosynthesisProtein Structure, SecondaryRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptidyl TransferasesRibosomal ProteinsRPL39 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsNewly Synthesized PolypeptidesProtein FoldingProtein SynthesisRibosomesSite-specific Cross-linkingTranslationYeast

Identifiers

PMID24072706
PMCPMC3837115
OpenAlexW2041342184

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.