Evidence map›Paper›PMID 22923520›Full record

ArticleNucleic acids research2012

Recognition of the 70S ribosome and polysome by the RNA degradosome in Escherichia coli.

Yi-Chun Tsai, Dijun Du, Lilianha Domínguez-Malfavón, Daniela Dimastrogiovanni, Jonathan Cross, Anastasia J Callaghan, Jaime García-Mena, Ben F Luisi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.5field-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

42 citing papers in PubMed, 70 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Yi-Chun TsaiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Dijun Du
Lilianha Domínguez-Malfavón
Daniela Dimastrogiovanni
Jonathan Cross
Anastasia J Callaghan
Jaime García-Mena
Ben F Luisi
University of Portsmouth · GBUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F013140/1Wellcome Trust
6 · The paper itself

Abstract

The RNA degradosome is a multi-enzyme assembly that contributes to key processes of RNA metabolism, and it engages numerous partners in serving its varied functional roles. Small domains within the assembly recognize collectively a diverse range of macromolecules, including the core protein components, the cytoplasmic lipid membrane, mRNAs, non-coding regulatory RNAs and precursors of structured RNAs. We present evidence that the degradosome can form a stable complex with the 70S ribosome and polysomes, and we demonstrate the proximity in vivo of ribosomal proteins and the scaffold of the degradosome, RNase E. The principal interactions are mapped to two, independent, RNA-binding domains from RNase E. RhlB, the RNA helicase component of the degradosome, also contributes to ribosome binding, and this is favoured through an activating interaction with RNase E. The catalytic activity of RNase E for processing 9S RNA (the ribosomal 5S RNA precursor) is repressed in the presence of the ribosome, whereas there is little affect on the cleavage of single-stranded substrates mediated by non-coding RNA, suggestings that the enzyme retains capacity to cleave unstructured substrates when associated with the ribosome. We propose that polysomes may act as antennae that enhance the rates of capture of the limited number of degradosomes, so that they become recruited to sites of active translation to act on mRNAs as they become exposed or tagged for degradation.

Indexed as

Binding SitesCross-Linking ReagentsDEAD-box RNA HelicasesEndoribonucleasesEscherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferMultienzyme ComplexesPolyribonucleotide NucleotidyltransferasePolyribosomesProtein Interaction Domains and MotifsRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialRNACross-Linking ReagentsDEAD-box RNA HelicasesdegradosomeEndoribonucleasesEscherichia coli ProteinsMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseRhlB protein, E coliribonuclease ERibosomal ProteinsRNARNA HelicasesRNA, Small Untranslated

Identifiers

PMID22923520
PMCPMC3488216
OpenAlexW2132737606

What OpenQuestion holds

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LicenceCC BY-NC
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.