Evidence map›Paper›PMID 27834591›Full record

ReviewRNA biology2017

Viral interference of the bacterial RNA metabolism machinery.

Tom Dendooven, An Van den Bossche, Hanne Hendrix, Pieter-Jan Ceyssens, Marleen Voet, K J Bandyra, Marc De Maeyer, Abram Aertsen, Jean-Paul Noben, Steven W Hardwick and 2 more

Open access · bronzeAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in RNA biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. 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

12 authors at 4 institutions in 2 countries.

Tom Dendoovena Laboratory of Gene Technology , KU Leuven , Leuven , Belgium.
An Van den Bosschea Laboratory of Gene Technology , KU Leuven , Leuven , Belgium.
Hanne Hendrixa Laboratory of Gene Technology , KU Leuven , Leuven , Belgium.
Pieter-Jan Ceyssensa Laboratory of Gene Technology , KU Leuven , Leuven , Belgium.
Marleen Voeta Laboratory of Gene Technology , KU Leuven , Leuven , Belgium.
K J Bandyrab Department of Biochemistry , University of Cambridge , Cambridge , UK.
Marc De Maeyerd Biochemistry, Molecular and Structural Biology Section , KU Leuven , Leuven , Belgium.
Abram Aertsene Laboratory of Food Microbiology , KU Leuven , Leuven , Belgium.
Jean-Paul Nobenf Biomedical Research Institute and Transnational University Limburg, Hasselt University , Diepenbeek , Belgium.
Steven W Hardwickb Department of Biochemistry , University of Cambridge , Cambridge , UK.
Ben F Luisib Department of Biochemistry , University of Cambridge , Cambridge , UK.
Rob Lavignea Laboratory of Gene Technology , KU Leuven , Leuven , Belgium.
KU Leuven · BEUniversity of Cambridge · GBHasselt University · BEInstitut Scientifique de Santé Publique · BE

Funding

Wellcome Trust 200873/Z/16/Z
6 · The paper itself

Abstract

In a recent publication, we reported a unique interaction between a protein encoded by the giant myovirus phiKZ and the Pseudomonas aeruginosa RNA degradosome. Crystallography, site-directed mutagenesis and interactomics approaches revealed this 'degradosome interacting protein' or Dip, to adopt an 'open-claw' dimeric structure that presents acidic patches on its outer surface which hijack 2 conserved RNA binding sites on the scaffold domain of the RNase E component of the RNA degradosome. This interaction prevents substrate RNAs from being bound and degraded by the RNA degradosome during the virus infection cycle. In this commentary, we provide a perspective into the biological role of Dip, its structural analysis and its mysterious evolutionary origin, and we suggest some therapeutic and biotechnological applications of this distinctive viral protein.

Indexed as

BacteriaBacteriophagesEndoribonucleasesHost-Pathogen InteractionsMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseProtein BindingPseudomonas aeruginosaRNA, BacterialRNA HelicasesRNA StabilitydegradosomeEndoribonucleasesMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseRNA, BacterialRNA HelicasesBacteriophagephage-host interactionPseudomonas aeruginosaRNA degradosomeRNase E

Identifiers

PMID27834591
PMCPMC5270514
OpenAlexW2557059746

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.