Evidence map›Paper›PMID 33330923›Full record

ArticleNucleic acids research2021

The versatile interactome of chloroplast ribosomes revealed by affinity purification mass spectrometry.

Lisa Désirée Westrich, Vincent Leon Gotsmann, Claudia Herkt, Fabian Ries, Tanja Kazek, Raphael Trösch, Laura Armbruster, Jens Stephan Mühlenbeck, Silvia Ramundo, Jörg Nickelsen and 5 more

Open access · goldAbstract readValidation Study
In one paragraph

Article in Nucleic acids research, 2021. 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
2.0field-weighted citation impact, top 13% 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, 35 citations in OpenAlex.

  1. Article
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  4. Plant MutS2 proteins function in plastid ribosome quality control.bioRxiv : the preprint server for biology · 2025
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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

15 authors at 5 institutions in 2 countries.

Lisa Désirée WestrichMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Str. 23, 67663 Kaiserslautern, Germany.
Vincent Leon GotsmannMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Str. 23, 67663 Kaiserslautern, Germany.
Claudia HerktMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Str. 23, 67663 Kaiserslautern, Germany.
Fabian RiesMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Str. 23, 67663 Kaiserslautern, Germany.
Tanja KazekMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Str. 23, 67663 Kaiserslautern, Germany.
Raphael TröschMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Str. 23, 67663 Kaiserslautern, Germany.
Laura ArmbrusterCentre for Organismal Studies, University of Heidelberg, Im Neuenheimer Feld 360, 69120 Heidelberg, Germany.
Jens Stephan MühlenbeckPlant Physiology, Institute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 7, 48149 Münster, Germany.
Silvia RamundoDepartment of Biochemistry and Biophysics, University of California, 600 16th St, N316, San Francisco, CA 94143, USA.
Jörg NickelsenDepartment of Molecular Plant Science, University of Munich, Grosshaderner-Str. 2-4, 82152 Planegg-Martinsried, Germany.
Iris FinkemeierPlant Physiology, Institute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 7, 48149 Münster, Germany.
Markus WirtzCentre for Organismal Studies, University of Heidelberg, Im Neuenheimer Feld 360, 69120 Heidelberg, Germany.
Zuzana StorchováMolecular Genetics, University of Kaiserslautern, Paul-Ehrlich-Str. 24, 67663 Kaiserslautern, Germany.
Markus RäschleMolecular Genetics, University of Kaiserslautern, Paul-Ehrlich-Str. 24, 67663 Kaiserslautern, Germany.
Felix WillmundMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Str. 23, 67663 Kaiserslautern, Germany.
University of Kaiserslautern · DEHeidelberg University · DEUniversity of Münster · DELudwig-Maximilians-Universität München · DEUniversity of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plant cells, chloroplast gene expression is predominantly controlled through post-transcriptional regulation. Such fine-tuning is vital for precisely orchestrating protein complex assembly as for the photosynthesis machinery and for quickly responding to environmental changes. While regulation of chloroplast protein synthesis is of central importance, little is known about the degree and nature of the regulatory network, mainly due to challenges associated with the specific isolation of transient ribosome interactors. Here, we established a ribosome affinity purification method, which enabled us to broadly uncover putative ribosome-associated proteins in chloroplasts. Endogenously tagging of a protein of the large or small subunit revealed not only interactors of the holo complex, but also preferential interactors of the two subunits. This includes known canonical regulatory proteins as well as several new proteins belonging to the categories of protein and RNA regulation, photosystem biogenesis, redox control and metabolism. The sensitivity of the here applied screen was validated for various transiently interacting proteins. We further provided evidence for the existence of a ribosome-associated Nα-acetyltransferase in chloroplasts and its ability to acetylate substrate proteins at their N-terminus. The broad set of ribosome interactors underscores the potential to regulate chloroplast gene expression on the level of protein synthesis.

Indexed as

AcetylationAmino Acid SequenceArabidopsisCell FractionationChlamydomonas reinhardtiiChloroplast ProteinsChloroplastsGene Expression Regulation, PlantImmunomagnetic SeparationMass SpectrometryModels, MolecularN-Terminal AcetyltransferasesPlant ProteinsProtein Processing, Post-TranslationalRibosomesRibosome Subunits, LargeChloroplast ProteinsN-Terminal AcetyltransferasesPlant Proteins

Identifiers

PMID33330923
PMCPMC7797057
OpenAlexW3112570663

What OpenQuestion holds

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LicenceCC BY-NC
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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.