Evidence map›Paper›PMID 28453818›Full record

ArticleNucleic acids research2017

Downstream element determines RNase Y cleavage of the saePQRS operon in Staphylococcus aureus.

Gabriella Marincola, Christiane Wolz

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Membrane Localization of RNase Y Is Important for Global Gene Expression inInternational journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
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  9. Article
  10. The Accessory GeneFrontiers in microbiology · 2020
    Article
  11. Article
  12. Article
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  14. 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

2 authors at 1 institution in 1 country.

Gabriella MarincolaInterfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, Tübingen 72076, Germany.
Christiane WolzInterfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, Tübingen 72076, Germany.
University of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In gram-positive bacteria, RNase J1, RNase J2 and RNase Y are thought to be major contributors to mRNA degradation and maturation. In Staphylococcus aureus, RNase Y activity is restricted to regulating the mRNA decay of only certain transcripts. Here the saePQRS operon was used as a model to analyze RNase Y specificity in living cells. A RNase Y cleavage site is located in an intergenic region between saeP and saeQ. This cleavage resulted in rapid degradation of the upstream fragment and stabilization of the downstream fragment. Thereby, the expression ratio of the different components of the operon was shifted towards saeRS, emphasizing the regulatory role of RNase Y activity. To assess cleavage specificity different regions surrounding the sae CS were cloned upstream of truncated gfp, and processing was analyzed in vivo using probes up- and downstream of CS. RNase Y cleavage was not determined by the cleavage site sequence. Instead a 24-bp double-stranded recognition structure was identified that was required to initiate cleavage 6 nt upstream. The results indicate that RNase Y activity is determined by secondary structure recognition determinants, which guide cleavage from a distance.

Indexed as

Bacterial ProteinsBase SequenceDNA, IntergenicEndoribonucleasesGene Expression Regulation, BacterialMultienzyme ComplexesMutagenesis, Site-DirectedNucleic Acid ConformationOperonPlasmidsPolyribonucleotide NucleotidyltransferaseProtein KinasesRecombinant Fusion ProteinsRegulatory Sequences, Nucleic AcidRNA, BacterialRNA HelicasesBacterial ProteinsdegradosomeDNA, IntergenicEndoribonucleasesMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseProtein KinasesRecombinant Fusion ProteinsRNA, BacterialRNA HelicasesRNA, MessengerSaeR protein, Staphylococcus aureusSaeS protein, Staphylococcus aureusTranscription Factors

Identifiers

PMID28453818
PMCPMC5449607
OpenAlexW2608187191

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.