Evidence map›Paper›PMID 40096066›Full record

ArticlePLoS genetics2025

Critical functions and key interactions mediated by the RNase E scaffolding domain in Pseudomonas aeruginosa.

Sandra Amandine Marie Geslain, Stéphane Hausmann, Johan Geiser, George Edward Allen, Diego Gonzalez, Martina Valentini

Abstract read
In one paragraph

Article in PLoS genetics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. 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

6 authors.

Sandra Amandine Marie GeslainDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.
Stéphane HausmannDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.
Johan GeiserDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0003-0046-1723
George Edward AllenDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.
Diego GonzalezLaboratory of Microbiology, University of Neuchâtel, Neuchâtel, Switzerland.ORCID https://orcid.org/0000-0003-3414-1461
Martina ValentiniDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNA degradosome is a bacterial multi-protein complex mediating mRNA processing and degradation. In Pseudomonadota, this complex assembles on the C-terminal domain (CTD) of RNase E through short linear motifs (SLiMs) that determine its composition and functionality. In the human pathogen Pseudomonas aeruginosa, the RNase E CTD exhibits limited similarity to that of model organisms, impeding our understanding of RNA metabolic processes in this bacterium. Our study systematically maps the interactions mediated by the P. aeruginosa RNase E CTD and highlights its critical role in transcript regulation and cellular functions. We identified the SLiMs crucial for membrane attachment, RNA binding and complex clustering, as well as for direct binding to the core components PNPase and RhlB. Transcriptome analyses of RNase E CTD mutants revealed altered expression of genes involved in quorum sensing, type III secretion, and amino acid metabolism. Additionally, we show that the mutants are impaired in cold adaptation, pH response, and virulence in an infection model. Overall, this work establishes the essential role of the RNA degradosome in driving bacterial adaptability and pathogenicity.

Indexed as

Bacterial ProteinsEndoribonucleasesPseudomonas aeruginosaGene Expression Regulation, BacterialHumansMultienzyme ComplexesMutationPolyribonucleotide NucleotidyltransferaseProtein DomainsPseudomonas InfectionsQuorum SensingRNA, BacterialRNA HelicasesVirulenceBacterial ProteinsdegradosomeEndoribonucleasesMultienzyme ComplexesPolyribonucleotide Nucleotidyltransferaseribonuclease ERNA, BacterialRNA Helicases

Identifiers

PMID40096066
PMCPMC11964227

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.