Evidence map›Paper›PMID 36834906›Full record

ArticleInternational journal of molecular sciences2023

Purification and Characterization of Authentic 30S Ribosomal Precursors Induced by Heat Shock.

Emmanuel Giudice, Sylvie Georgeault, Régis Lavigne, Charles Pineau, Annie Trautwetter, Gwennola Ermel, Carlos Blanco, Reynald Gillet

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

8 authors at 5 institutions in 1 country.

Emmanuel GiudiceUniv Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France.
Sylvie GeorgeaultUniv Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France.
Régis LavigneUniv Rennes, Inserm, EHESP, Irset (Institut de Recherche en Santé, Environnement et Travail)-UMR_S 1085, 35000 Rennes, France.
Charles PineauUniv Rennes, Inserm, EHESP, Irset (Institut de Recherche en Santé, Environnement et Travail)-UMR_S 1085, 35000 Rennes, France.
Annie TrautwetterUniv Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France.
Gwennola ErmelUniv Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France.
Carlos BlancoUniv Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France.
Reynald GilletUniv Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France.
Institut de génétique et de développement de Rennes · FRCentre National de la Recherche Scientifique · FRInserm · FRInstitut de Recherche en Santé, Environnement et Travail · FRUniversité de Rennes · FR

Funding

Agence Nationale pour la Recherche (ANR)/Direction Générale de l'Armement ANR-14-ASTR-0001Fondation pour la Recherche Médicale Equipe FRM EQU202203014663
6 · The paper itself

Abstract

Ribosome biogenesis is a complex and multistep process that depends on various assembly factors. To understand this process and identify the ribosome assembly intermediates, most studies have set out to delete or deplete these assembly factors. Instead, we took advantage of the impact of heat stress (45 °C) on the late stages of the biogenesis of the 30S ribosomal subunit to explore authentic precursors. Under these conditions, reduced levels of the DnaK chaperone proteins devoted to ribosome assembly lead to the transient accumulation of 21S ribosomal particles, which are 30S precursors. We constructed strains with different affinity tags on one early and one late 30S ribosomal protein and purified the 21S particles that form under heat shock. A combination of relative quantification using mass spectrometry-based proteomics and cryo-electron microscopy (cryo-EM) was then used to determine their protein contents and structures.

Indexed as

Escherichia coliEscherichia coli ProteinsCryoelectron MicroscopyHeat-Shock ResponseHSP70 Heat-Shock ProteinsRibosomal ProteinsRibosomesEscherichia coli ProteinsHSP70 Heat-Shock ProteinsRibosomal Proteins21Scryo-EMDnaKheat shockribosome assembly

Identifiers

PMID36834906
PMCPMC9959188
OpenAlexW4319985468

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.