Evidence map›Paper›PMID 28180335›Full record

ArticleNucleic acids research2017

Sinorhizobium meliloti YbeY is an endoribonuclease with unprecedented catalytic features, acting as silencing enzyme in riboregulation.

Margarida Saramago, Alexandra Peregrina, Marta Robledo, Rute G Matos, Rolf Hilker, Javier Serrania, Anke Becker, Cecilia M Arraiano, José I Jiménez-Zurdo

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
8.2field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. SARS-CoV2 Nsp1 is a metal-dependent DNA and RNA endonuclease.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
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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

9 authors at 4 institutions in 3 countries.

Margarida SaramagoInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, Oeiras, Portugal.
Alexandra PeregrinaGrupo de Ecología Genética de la Rizosfera, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), Granada, Spain.
Marta RobledoGrupo de Ecología Genética de la Rizosfera, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), Granada, Spain.
Rute G MatosInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, Oeiras, Portugal.
Rolf HilkerLOEWE Center for Synthetic Microbiology and Faculty of Biology, Philipps-University Marburg, Marburg, Germany.
Javier SerraniaLOEWE Center for Synthetic Microbiology and Faculty of Biology, Philipps-University Marburg, Marburg, Germany.
Anke BeckerLOEWE Center for Synthetic Microbiology and Faculty of Biology, Philipps-University Marburg, Marburg, Germany.
Cecilia M ArraianoInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, Oeiras, Portugal.
José I Jiménez-ZurdoGrupo de Ecología Genética de la Rizosfera, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), Granada, Spain.
Loewe Center for Synthetic Microbiology · DEUniversidade Nova de Lisboa · PTConsejo Superior de Investigaciones Científicas · ESEstación Experimental del Zaidín · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural and biochemical features suggest that the almost ubiquitous bacterial YbeY protein may serve catalytic and/or Hfq-like protective functions central to small RNA (sRNA)-mediated regulation and RNA metabolism. We have biochemically and genetically characterized the YbeY ortholog of the legume symbiont Sinorhizobium meliloti (SmYbeY). Co-immunoprecipitation (CoIP) with a FLAG-tagged SmYbeY yielded a poor enrichment in RNA species, compared to Hfq CoIP-RNA uncovered previously by a similar experimental setup. Purified SmYbeY behaved as a monomer that indistinctly cleaved single- and double-stranded RNA substrates, a unique ability among bacterial endoribonucleases. SmYbeY-mediated catalysis was supported by the divalent metal ions Mg2+, Mn2+ and Ca2+, which influenced in a different manner cleavage efficiency and reactivity patterns, with Ca2+ specifically blocking activity on double-stranded and some structured RNA molecules. SmYbeY loss-of-function compromised expression of core energy and RNA metabolism genes, whilst promoting accumulation of motility, late symbiotic and transport mRNAs. Some of the latter transcripts are known Hfq-binding sRNA targets and might be SmYbeY substrates. Genetic reporter and in vitro assays confirmed that SmYbeY is required for sRNA-mediated down-regulation of the amino acid ABC transporter prbA mRNA. We have thus discovered a bacterial endoribonuclease with unprecedented catalytic features, acting also as gene silencing enzyme.

Indexed as

Amino Acid SubstitutionATP-Binding Cassette TransportersBacterial ProteinsBase SequenceCatalysisChromosomes, BacterialEndoribonucleasesGene DeletionGene Expression ProfilingGenes, BacterialGene SilencingGenes, ReporterHost Factor 1 ProteinMetalloproteinsMutagenesis, Site-DirectedNucleic Acid ConformationATP-Binding Cassette TransportersBacterial ProteinsEndoribonucleasesHost Factor 1 ProteinMetalloproteinsRecombinant ProteinsRNA, Bacterial

Identifiers

PMID28180335
PMCPMC5388416
OpenAlexW2560832692

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.