Evidence map›Paper›PMID 32245971›Full record

ArticleNature communications2020

Mechanism of ribosome shutdown by RsfS in Staphylococcus aureus revealed by integrative structural biology approach.

Iskander Khusainov, Bulat Fatkhullin, Simone Pellegrino, Aydar Bikmullin, Wen-Ti Liu, Azat Gabdulkhakov, Amr Al Shebel, Alexander Golubev, Denis Zeyer, Natalie Trachtmann and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  3. Mechanistic insights intobioRxiv : the preprint server for biology · 2026
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  15. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity inInternational journal of molecular sciences · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

15 authors at 4 institutions in 4 countries.

Iskander Khusainov *Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia. iskander.khusainov@biophys.mpg.de.ORCID http://orcid.org/0000-0001-5199-5157
Bulat Fatkhullin *Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia.
Simone Pellegrino *Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, INSERM, U964, CNRS, UMR7104, University of Strasbourg, 1 rue Laurent Fries, F-67400, Illkirch, France.ORCID http://orcid.org/0000-0001-6302-2774
Aydar Bikmullin *Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia.
Wen-Ti LiuNovAliX, BioParc, 850 bld Sebastien Brant, 67400, Illkirch, France.
Azat GabdulkhakovInstitute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290, Puschino, Moscow Region, Russian Federation.
Amr Al ShebelLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia.ORCID http://orcid.org/0000-0001-7459-3839
Alexander GolubevLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia.
Denis ZeyerNovAliX, BioParc, 850 bld Sebastien Brant, 67400, Illkirch, France.
Natalie TrachtmannLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia.
Georg A SprengerInstitute of Microbiology, University of Stuttgart, Allmandring 31, Stuttgart, 70569, Germany.ORCID http://orcid.org/0000-0002-7879-8978
Shamil ValidovLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia.
Konstantin UsachevLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia.
Gulnara YusupovaDepartment of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, INSERM, U964, CNRS, UMR7104, University of Strasbourg, 1 rue Laurent Fries, F-67400, Illkirch, France. gula@igbmc.fr.
Marat YusupovLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kremlyovskaya Street 18, Kazan, 420008, Russia. marat@igbmc.fr.
Centre National de la Recherche Scientifique · FRKazan Federal University · RUUniversity of Stuttgart · DEInstitute of Protein Research · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the sake of energy preservation, bacteria, upon transition to stationary phase, tone down their protein synthesis. This process is favored by the reversible binding of small stress-induced proteins to the ribosome to prevent unnecessary translation. One example is the conserved bacterial ribosome silencing factor (RsfS) that binds to uL14 protein onto the large ribosomal subunit and prevents its association with the small subunit. Here we describe the binding mode of Staphylococcus aureus RsfS to the large ribosomal subunit and present a 3.2 Å resolution cryo-EM reconstruction of the 50S-RsfS complex together with the crystal structure of uL14-RsfS complex solved at 2.3 Å resolution. The understanding of the detailed landscape of RsfS-uL14 interactions within the ribosome shed light on the mechanism of ribosome shutdown in the human pathogen S. aureus and might deliver a novel target for pharmacological drug development and treatment of bacterial infections.

Indexed as

Bacterial ProteinsCryoelectron MicroscopyCrystallography, X-RayDrug DevelopmentProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryRibosomal ProteinsRibosomesRibosome SubunitsStaphylococcus aureusBacterial ProteinsRibosomal Proteins

Identifiers

PMID32245971
PMCPMC7125091
OpenAlexW3014900997

What OpenQuestion holds

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LicenceCC BY
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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.