Evidence map›Paper›PMID 28878399›Full record

ArticleScientific reports2017

Structural and molecular comparison of bacterial and eukaryotic trigger factors.

Fabian Ries, Yvonne Carius, Marina Rohr, Karin Gries, Sandro Keller, C Roy D Lancaster, Felix Willmund

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  7. Structural features of chloroplast trigger factor determined at 2.6 Å resolution.Acta crystallographica. Section D, Structural biology · 2022
    Article
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  13. Review
  14. ThePlant physiology · 2019
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  17. Review
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

7 authors at 2 institutions in 1 country.

Fabian RiesMolecular Genetics of Eukaryotes, University of Kaiserslautern, Erwin-Schrödinger-Str. 70, 67663, Kaiserslautern, Germany.
Yvonne CariusDepartment of Structural Biology, Saarland University, Center of Human and Molecular Biology (ZHMB), Faculty of Medicine Building 60, 66421, Homburg, Germany.
Marina RohrMolecular Genetics of Eukaryotes, University of Kaiserslautern, Erwin-Schrödinger-Str. 70, 67663, Kaiserslautern, Germany.
Karin GriesMolecular Genetics of Eukaryotes, University of Kaiserslautern, Erwin-Schrödinger-Str. 70, 67663, Kaiserslautern, Germany.
Sandro KellerMolecular Biophysics, University of Kaiserslautern, Erwin-Schrödinger-Str. 13, 67663, Kaiserslautern, Germany.
C Roy D LancasterDepartment of Structural Biology, Saarland University, Center of Human and Molecular Biology (ZHMB), Faculty of Medicine Building 60, 66421, Homburg, Germany. Roy.Lancaster@structural-biology.eu.
Felix WillmundMolecular Genetics of Eukaryotes, University of Kaiserslautern, Erwin-Schrödinger-Str. 70, 67663, Kaiserslautern, Germany. willmund@bio.uni-kl.de.
University of Kaiserslautern · DESaarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A considerably small fraction of approximately 60-100 proteins of all chloroplast proteins are encoded by the plastid genome. Many of these proteins are major subunits of complexes with central functions within plastids. In comparison with other subcellular compartments and bacteria, many steps of chloroplast protein biogenesis are not well understood. We report here on the first study of chloroplast-localised trigger factor. In bacteria, this molecular chaperone is known to associate with translating ribosomes to facilitate the folding of newly synthesized proteins. Chloroplast trigger factors of the unicellular green algae Chlamydomonas reinhardtii and the vascular land plant Arabidopsis thaliana were characterized by biophysical and structural methods and compared to the Escherichia coli isoform. We show that chloroplast trigger factor is mainly monomeric and displays only moderate stability against thermal unfolding even under mild heat-stress conditions. The global shape and conformation of these proteins were determined in solution by small-angle X-ray scattering and subsequent ab initio modelling. As observed for bacteria, plastidic trigger factors have a dragon-like structure, albeit with slightly altered domain arrangement and flexibility. This structural conservation despite low amino acid sequence homology illustrates a remarkable evolutionary robustness of chaperone conformations across various kingdoms of life.

Indexed as

Bacterial Physiological PhenomenaAmino Acid SequenceBacterial ProteinsChloroplastsEukaryotaEvolution, MolecularModels, MolecularMolecular ConformationPhylogenyProtein MultimerizationStructure-Activity RelationshipThermodynamicsBacterial Proteins

Identifiers

PMID28878399
PMCPMC5587573
OpenAlexW2752143406

What OpenQuestion holds

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Registered trials

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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.