Evidence map›Paper›PMID 31114879›Full record

ArticleNucleic acids research2019

A dual role of the ribosome-bound chaperones RAC/Ssb in maintaining the fidelity of translation termination.

Anne-Sophie Gribling-Burrer, Marco Chiabudini, Ying Zhang, Zonghao Qiu, Mario Scazzari, Tina Wölfle, Daniel Wohlwend, Sabine Rospert

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Anne-Sophie Gribling-BurrerInstitute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
Marco ChiabudiniInstitute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
Ying ZhangInstitute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
Zonghao QiuInstitute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
Mario ScazzariInstitute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
Tina WölfleInstitute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
Daniel WohlwendInstitute of Biochemistry, Chemical and Pharmaceutical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
Sabine RospertInstitute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, D-79104 Freiburg, Germany.
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast ribosome-associated complex RAC and the Hsp70 homolog Ssb are anchored to the ribosome and together act as chaperones for the folding and co-translational assembly of nascent polypeptides. In addition, the RAC/Ssb system plays a crucial role in maintaining the fidelity of translation termination; however, the latter function is poorly understood. Here we show that the RAC/Ssb system promotes the fidelity of translation termination via two distinct mechanisms. First, via direct contacts with the ribosome and the nascent chain, RAC/Ssb facilitates the translation of stalling-prone poly-AAG/A sequences encoding for polylysine segments. Impairment of this function leads to enhanced ribosome stalling and to premature nascent polypeptide release at AAG/A codons. Second, RAC/Ssb is required for the assembly of fully functional ribosomes. When RAC/Ssb is absent, ribosome biogenesis is hampered such that core ribosomal particles are structurally altered at the decoding and peptidyl transferase centers. As a result, ribosomes assembled in the absence of RAC/Ssb bind to the aminoglycoside paromomycin with high affinity (KD = 76.6 nM) and display impaired discrimination between stop codons and sense codons. The combined data shed light on the multiple mechanisms by which the RAC/Ssb system promotes unimpeded biogenesis of newly synthesized polypeptides.

Indexed as

CodonCodon, TerminatorMolecular ChaperonesMultiprotein ComplexesNucleic Acid ConformationOrganelle BiogenesisParomomycinPeptide Chain Termination, TranslationalPolylysineRibosomesRNA, RibosomalSaccharomyces cerevisiae ProteinsCodonCodon, TerminatorMolecular ChaperonesMultiprotein ComplexesParomomycinPolylysineRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID31114879
PMCPMC6648330
OpenAlexW2944979277

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.