Evidence map›Paper›PMID 30486791›Full record

ArticleBMC genomics2018

PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli.

Clémentine Dressaire, Vânia Pobre, Sandrine Laguerre, Laurence Girbal, Cecilia Maria Arraiano, Muriel Cocaign-Bousquet

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2018. 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
1.4field-weighted citation impact, top 16% 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, 22 citations in OpenAlex.

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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.

Clémentine DressaireInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157, Oeiras, Portugal.
Vânia PobreInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157, Oeiras, Portugal.
Sandrine LaguerreLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Laurence GirbalLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France. girbal@insa-toulouse.fr.ORCID http://orcid.org/0000-0002-8773-4829
Cecilia Maria ArraianoInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157, Oeiras, Portugal. cecilia@itqb.unl.pt.
Muriel Cocaign-BousquetLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Centre National de la Recherche Scientifique · FRInstituto de Biologia Experimental e Tecnológica · PT

Funding

European Union's Horizon 2020 research and innovation program No 635536FCT Post-Doctoral Fellowships SFRH/BPD/65528/2009FCT Post-Doctoral Fellowships SFRH/BPD/87188/2012FEDER funds PTDC/BIA-MIC/1399/2014Fundação para a Ciência e Tecnologia (FCT-Portugal) LISBOA-01-0145-FEDER-007660
6 · The paper itself

Abstract

backgroundExoribonucleases are crucial for RNA degradation in Escherichia coli but the roles of RNase R and PNPase and their potential overlap in stationary phase are not well characterized. Here, we used a genome-wide approach to determine how RNase R and PNPase affect the mRNA half-lives in the stationary phase. The genome-wide mRNA half-lives were determined by a dynamic analysis of transcriptomes after transcription arrest. We have combined the analysis of mRNA half-lives with the steady-state concentrations (transcriptome) to provide an integrated overview of the in vivo activity of these exoribonucleases at the genome-scale.

resultsThe values of mRNA half-lives demonstrated that the mRNAs are very stable in the stationary phase and that the deletion of RNase R or PNPase caused only a limited mRNA stabilization. Intriguingly the absence of PNPase provoked also the destabilization of many mRNAs. These changes in mRNA half-lives in the PNPase deletion strain were associated with a massive reorganization of mRNA levels and also variation in several ncRNA concentrations. Finally, the in vivo activity of the degradation machinery was found frequently saturated by mRNAs in the PNPase mutant unlike in the RNase R mutant, suggesting that the degradation activity is limited by the deletion of PNPase but not by the deletion of RNase R.

conclusionsThis work had identified PNPase as a central player associated with mRNA degradation in stationary phase.

Indexed as

RNA StabilityEscherichia coliExoribonucleasesGenome, BacterialHalf-LifeMutationRNA, MessengerRNA, UntranslatedTranscriptomeExoribonucleasesribonuclease RRNA, MessengerRNA, UntranslatedE. coliGene expression regulationPNPaseRNA decayRNase RTranscriptome

Identifiers

PMID30486791
PMCPMC6264599
OpenAlexW2902327213

What OpenQuestion holds

Textmetadata
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.