Evidence map›Paper›PMID 29136196›Full record

ArticleNucleic acids research2018

Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes.

Heather A Bruce, Dijun Du, Dijana Matak-Vinkovic, Katarzyna J Bandyra, R William Broadhurst, Esther Martin, Frank Sobott, Alexander V Shkumatov, Ben F Luisi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 56 citations in OpenAlex.

  1. Mapping of RNA Helicase Dynamics by HDX-MS.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Article
  3. Article
  4. Article
  5. What makes a small RNA work?Nucleic acids research · 2025
    Review
  6. Article
  7. Article
  8. Article
  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
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021
    Review
  19. Article
  20. 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 4 institutions in 2 countries.

Heather A BruceDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Dijun DuDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Dijana Matak-VinkovicDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Katarzyna J BandyraDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
R William BroadhurstDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Esther MartinBiomolecular & Analytical Mass Spectrometry group, Department of Chemistry, University of Antwerp, 2020 Antwerp, Belgium.
Frank SobottBiomolecular & Analytical Mass Spectrometry group, Department of Chemistry, University of Antwerp, 2020 Antwerp, Belgium.
Alexander V ShkumatovStructural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
University of Cambridge · GBUniversity of Antwerp · BEUniversity of Leeds · GBVIB-VUB Center for Structural Biology · BE

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 200873/Z/16/Z
6 · The paper itself

Abstract

The RNA degradosome is a multi-enzyme assembly that plays a central role in the RNA metabolism of Escherichia coli and numerous other bacterial species including pathogens. At the core of the assembly is the endoribonuclease RNase E, one of the largest E. coli proteins and also one that bears the greatest region predicted to be natively unstructured. This extensive unstructured region, situated in the C-terminal half of RNase E, is punctuated with conserved short linear motifs that recruit partner proteins, direct RNA interactions, and enable association with the cytoplasmic membrane. We have structurally characterized a subassembly of the degradosome-comprising a 248-residue segment of the natively unstructured part of RNase E, the DEAD-box helicase RhlB and the glycolytic enzyme enolase, and provide evidence that it serves as a flexible recognition centre that can co-recruit small regulatory RNA and the RNA chaperone Hfq. Our results support a model in which the degradosome captures substrates and regulatory RNAs through the recognition centre, facilitates pairing to cognate transcripts and presents the target to the ribonuclease active sites of the greater assembly for cooperative degradation or processing.

Indexed as

Binding SitesCrystallography, X-RayEndoribonucleasesEscherichia coli ProteinsHost Factor 1 ProteinModels, MolecularMultienzyme ComplexesNucleic Acid ConformationPolyribonucleotide NucleotidyltransferaseProtein BindingProtein DomainsRNA, BacterialRNA HelicasesdegradosomeEndoribonucleasesEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseRNA, BacterialRNA Helicases

Identifiers

PMID29136196
PMCPMC5758883
OpenAlexW2767429769

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.