Evidence map›Paper›PMID 28277929›Full record

ArticleRNA biology2017

Both exo- and endo-nucleolytic activities of RNase J1 from Staphylococcus aureus are manganese dependent and active on triphosphorylated 5'-ends.

Stéphane Hausmann, Vanessa Andrade Guimarães, Dominique Garcin, Natalia Baumann, Patrick Linder, Peter Redder

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  7. Structural and biochemical characteristics of twoThe Journal of biological chemistry · 2020
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  8. Review
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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

6 authors at 2 institutions in 2 countries.

Stéphane Hausmanna Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
Vanessa Andrade Guimarãesa Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
Dominique Garcina Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
Natalia Baumanna Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
Patrick Lindera Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
Peter Reddera Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
University of Geneva · CHLaboratoire de Microbiologie et Génétique Moléculaires · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA decay and RNA maturation are important steps in the regulation of bacterial gene expression. RNase J, which is present in about half of bacterial species, has been shown to possess both endo- and 5' to 3' exo-ribonuclease activities. The exonucleolytic activity is clearly involved in the degradation of mRNA and in the maturation of at least the 5' end of 16S rRNA in the 2 Firmicutes Staphylococcus aureus and Bacillus subtilis. The endoribonuclease activity of RNase J from several species has been shown to be weak in vitro and 3-D structural data of different RNase J orthologs have not provided a clear explanation for the molecular basis of this activity. Here, we show that S. aureus RNase J1 is a manganese dependent homodimeric enzyme with strong 5' to 3' exo-ribonuclease as well as endo-ribonuclease activity. In addition, we demonstrated that SauJ1 can efficiently degrade 5' triphosphorylated RNA. Our results highlight RNase J1 as an important player in RNA turnover in S. aureus.

Indexed as

Bacterial ProteinsCloning, MolecularGene Expression Regulation, BacterialManganesePhosphorylationProtein Structure, QuaternaryRibonucleasesStaphylococcus aureusBacterial ProteinsManganeseRibonucleasesEndoribonucleaseexoribonucleasemanganeseRNase J1S. aureustriphosphorylated RNA

Identifiers

PMID28277929
PMCPMC5711453
OpenAlexW2594194380

What OpenQuestion holds

Textmetadata
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.