Evidence map›Paper›PMID 22829778›Full record

ArticlePLoS genetics2012

RsfA (YbeB) proteins are conserved ribosomal silencing factors.

Roman Häuser, Markus Pech, Jaroslaw Kijek, Hiroshi Yamamoto, Björn Titz, Florian Naeve, Andrey Tovchigrechko, Kaori Yamamoto, Witold Szaflarski, Nono Takeuchi and 4 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

62 citing papers in PubMed, 108 citations in OpenAlex.

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  12. The maizePlant direct · 2024
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  15. Unveiling the inhibition mechanism ofFrontiers in microbiology · 2023
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  16. Article
  17. Article
  18. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity inInternational journal of molecular sciences · 2022
    Article
  19. A roadmap for the functional annotation of protein families: a community perspective.Database : the journal of biological databases and curation · 2022
    Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

14 authors at 6 institutions in 4 countries.

Roman HäuserInstitute of Toxicology and Genetics, Karlsruhe Institute of Technology, Karlsruhe, Germany.
Markus Pech
Jaroslaw Kijek
Hiroshi Yamamoto
Björn Titz
Florian Naeve
Andrey Tovchigrechko
Kaori Yamamoto
Witold Szaflarski
Nono Takeuchi
Thorsten Stellberger
Markus E Diefenbacher
Knud H Nierhaus
Peter Uetz
Karlsruhe Institute of Technology · DEMax Planck Institute for Molecular Genetics · DECharité - Universitätsmedizin Berlin · DEHeidelberg University · DEJ. Craig Venter Institute · USThe University of Tokyo · JP

Funding

A Protein-Protein Interaction Map of Escherichia coliR01GM079710 · NIGMS · J. CRAIG VENTER INSTITUTE, INC. · PI RAJAGOPALA, SEESANDRA VENKATAPPA · 2008 to 2011
$2.5M
NIGMS NIH HHS R01 GM079710NIGMS NIH HHS R01GM79710
6 · The paper itself

Abstract

The YbeB (DUF143) family of uncharacterized proteins is encoded by almost all bacterial and eukaryotic genomes but not archaea. While they have been shown to be associated with ribosomes, their molecular function remains unclear. Here we show that YbeB is a ribosomal silencing factor (RsfA) in the stationary growth phase and during the transition from rich to poor media. A knock-out of the rsfA gene shows two strong phenotypes: (i) the viability of the mutant cells are sharply impaired during stationary phase (as shown by viability competition assays), and (ii) during transition from rich to poor media the mutant cells adapt slowly and show a growth block of more than 10 hours (as shown by growth competition assays). RsfA silences translation by binding to the L14 protein of the large ribosomal subunit and, as a consequence, impairs subunit joining (as shown by molecular modeling, reporter gene analysis, in vitro translation assays, and sucrose gradient analysis). This particular interaction is conserved in all species tested, including Escherichia coli, Treponema pallidum, Streptococcus pneumoniae, Synechocystis PCC 6803, as well as human mitochondria and maize chloroplasts (as demonstrated by yeast two-hybrid tests, pull-downs, and mutagenesis). RsfA is unrelated to the eukaryotic ribosomal anti-association/60S-assembly factor eIF6, which also binds to L14, and is the first such factor in bacteria and organelles. RsfA helps cells to adapt to slow-growth/stationary phase conditions by down-regulating protein synthesis, one of the most energy-consuming processes in both bacterial and eukaryotic cells.

Indexed as

BacteriaEukaryotaBacterial ProteinsBinding SitesConserved SequenceHeLa CellsHumansMitochondriaMolecular Sequence DataPhylogenyProtein BindingProtein BiosynthesisRibosomal ProteinsRibosome Subunits, LargeSequence Homology, Amino AcidTranscription FactorsBacterial Proteinsribosomal protein L14Ribosomal ProteinsrsfA protein, Bacillus subtilisTranscription Factors

Identifiers

PMID22829778
PMCPMC3400551
OpenAlexW2000151385

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.