Evidence map›Paper›PMID 34415624›Full record

ArticleMolecular microbiology2022

Multi-scale ensemble properties of the Escherichia coli RNA degradosome.

Tom Dendooven, Giulia Paris, Alexander V Shkumatov, Md Saiful Islam, Alister Burt, Marta A Kubańska, Tai Yuchen Yang, Steven W Hardwick, Ben F Luisi

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. What makes a small RNA work?Nucleic acids research · 2025
    Review
  4. Article
  5. Article
  6. Selective 8-oxo-rG stalling occurs in the catalytic core of polynucleotide phosphorylase (PNPase) during degradation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Target recognition by RNase E RNA-binding domain AR2 drives sRNA decay in the absence of PNPase.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. 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

9 authors at 3 institutions in 3 countries.

Tom DendoovenDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-9847-0910
Giulia ParisDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-5610-2722
Alexander V ShkumatovCenter for Structural Biology, Vlaams Instituut voor Biotechnologie, Brussels, Belgium.
Md Saiful IslamDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Alister BurtInstitut de Biologie Structurale, Université Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
Marta A KubańskaDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Tai Yuchen YangDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Steven W HardwickDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0003-1144-9877
University of Cambridge · GBCentre National de la Recherche Scientifique · FRVrije Universiteit Brussel · BE

Funding

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

Abstract

In organisms from all domains of life, multi-enzyme assemblies play central roles in defining transcript lifetimes and facilitating RNA-mediated regulation of gene expression. An assembly dedicated to such roles, known as the RNA degradosome, is found amongst bacteria from highly diverse lineages. About a fifth of the assembly mass of the degradosome of Escherichia coli and related species is predicted to be intrinsically disordered - a property that has been sustained for over a billion years of bacterial molecular history and stands in marked contrast to the high degree of sequence variation of that same region. Here, we characterize the conformational dynamics of the degradosome using a hybrid structural biology approach that combines solution scattering with ad hoc ensemble modelling, cryo-electron microscopy, and other biophysical methods. The E. coli degradosome can form punctate bodies in vivo that may facilitate its functional activities, and based on our results, we propose an electrostatic switch model to account for the propensity of the degradosome to undergo programmable puncta formation.

Indexed as

EndoribonucleasesGene Expression Regulation, BacterialMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseRNA HelicasesCatalytic DomainCryoelectron MicroscopyElectrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsIntrinsically Disordered ProteinsModels, StructuralMutationRibonucleasesRNA, BacterialRNA Processing, Post-TranscriptionaldegradosomeEndoribonucleasesEscherichia coli ProteinsIntrinsically Disordered ProteinsMultienzyme ComplexesPolyribonucleotide Nucleotidyltransferaseribonuclease ERibonucleasesRNA, BacterialRNA Helicasescolloidal polymerintrinsically disordered proteinpost-transcriptional gene regulationribonucleaseriboregulationRNA condensatesRNA metabolismRNase ERNA surveillance

Identifiers

PMID34415624
PMCPMC7613265
OpenAlexW3195844999

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.