Evidence map›Paper›PMID 17179154›Full record

ArticleThe Journal of biological chemistry2007

Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1.

Reynald Gillet, Sukhjit Kaur, Wen Li, Marc Hallier, Brice Felden, Joachim Frank

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Joachim Frank's Binding with the Ribosome.Structure (London, England : 1993) · 2019
    Review
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  17. Functional SmpB-ribosome interactions require tmRNA.The Journal of biological chemistry · 2007
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  18. Article
  19. Article
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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

6 authors at 2 institutions in 2 countries.

Reynald GilletUniversité de Rennes I, IFR 140, UPRES JE 2311, INSERM U835 Biochimie Pharmaceutique, 2 Avenue du Professeur Léon Bernard, 35043 Rennes, France.
Sukhjit Kaur
Wen Li
Marc Hallier
Brice Felden
Joachim Frank
Inserm · FRWadsworth Center · US

Funding

STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLYR37GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2006
$2.8M
Structural studies on ribosomes and antibioticsR01GM067624 · NIGMS · MEDICAL RES COUNCIL LAB OF MOLEC BIOL · PI RAMAKRISHNAN, VENKATRAMAN · 2003 to 2006
$697k
NIGMS NIH HHS GM55440NIGMS NIH HHS GM 67624NIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM055440NIGMS NIH HHS R01 GM067624NIGMS NIH HHS R37 GM029169NIGMS NIH HHS R37 GM29169
6 · The paper itself

Abstract

A eubacterial ribosome stalled on a defective mRNA can be released through a quality control mechanism referred to as trans-translation, which depends on the coordinating binding actions of transfer-messenger RNA, small protein B, and ribosome protein S1. By means of cryo-electron microscopy, we obtained a map of the complex composed of a stalled ribosome and small protein B, which appears near the decoding center. This result suggests that, when lacking a codon, the A-site on the small subunit is a target for small protein B. To investigate the role of S1 played in trans-translation, we obtained a cryo-electron microscopic map, including a stalled ribosome, transfer-messenger RNA, and small protein Bs but in the absence of S1. In this complex, several connections between the 30 S subunit and transfer-messenger RNA that appear in the +S1 complex are no longer found. We propose the unifying concept of scaffolding for the roles of small protein B and S1 in binding of transfer-messenger RNA to the ribosome during trans-translation, and we infer a pathway of sequential binding events in the initial phase of trans-translation.

Indexed as

Protein BiosynthesisCryoelectron MicroscopyMacromolecular SubstancesProtein BindingRibosomal ProteinsRNA-Binding ProteinsRNA, TransferThermus thermophilusMacromolecular SubstancesRibosomal Proteinsribosomal protein S1RNA-Binding ProteinsRNA, Transfersmall protein B

Identifiers

PMID17179154
PMCPMC3230075
OpenAlexW1968628309

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.