Evidence map›Paper›PMID 11134527›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E.

G G Liou, W N Jane, S N Cohen, N S Lin, S Lin-Chao

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

74 citing papers in PubMed, 162 citations in OpenAlex.

  1. Dynamic partitioning shapes the in vivo organization of theProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Dynamic partitioning shapes thebioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. T-DNA insertion mutagenesis inMicrobiology (Reading, England) · 2023
    Article
  11. Article
  12. Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021
    Review
  13. Article
  14. Article
  15. Posttranscriptional Regulation ofJournal of bacteriology · 2020
    Article
  16. When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.Frontiers in cell and developmental biology · 2019
    Review
  17. Article
  18. Review
  19. RNA-binding proteins in bacteria.Nature reviews. Microbiology · 2018
    Review
  20. Review

14 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

G G LiouInstitute of Molecular Biology, Academia Sinica, Nankang, Taipei 115, Taiwan.
W N Jane
S N Cohen
N S Lin
S Lin-Chao
Institute of Molecular Biology, Academia Sinica · TWNational Taiwan University · TW

Funding

POLYADENYLATION OF RNA IN BACTERIAR01GM054158 · NIGMS · STANFORD UNIVERSITY · PI COHEN, STANLEY N · 1996 to 2006
$1.5M
NIGMS NIH HHS GM 54158NIGMS NIH HHS R01 GM054158
6 · The paper itself

Abstract

RNase E isolated from Escherichia coli is contained in a multicomponent "degradosome" complex with other proteins implicated in RNA decay. Earlier work has shown that the C-terminal region of RNase E is a scaffold for the binding of degradosome components and has identified specific RNase E segments necessary for its interaction with polynucleotide phosphorylase (PNPase), RhlB RNA helicase, and enolase. Here, we report electron microscopy studies that use immunogold labeling and freeze-fracture methods to show that degradosomes exist in vivo in E. coli as multicomponent structures that associate with the cytoplasmic membrane via the N-terminal region of RNase E. Whereas PNPase and enolase are present in E. coli in large excess relative to RNase E and therefore are detected in cells largely as molecules unlinked to the RNase E scaffold, immunogold labeling and biochemical analyses show that helicase is present in approximately equimolar amounts to RNase E at all cell growth stages. Our findings, which establish the existence and cellular location of RNase E-based degradosomes in vivo in E. coli, also suggest that RNA processing and decay may occur at specific sites within cells.

Indexed as

Bacterial ProteinsBlotting, WesternCell MembraneEndoribonucleasesEscherichia coliFreeze FracturingImmunohistochemistryMembrane ProteinsMicroscopy, ElectronMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseProtein BindingRNA, BacterialRNA HelicasesBacterial ProteinsdegradosomeEndoribonucleasesMembrane ProteinsMultienzyme ComplexesPolyribonucleotide Nucleotidyltransferaseribonuclease ERNA, BacterialRNA Helicases

Identifiers

PMID11134527
PMCPMC14545
OpenAlexW2061429937

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.