Evidence map›Paper›PMID 20005802›Full record

ArticleCell2009

The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE.

Cajetan Neubauer, Yong-Gui Gao, Kasper R Andersen, Christine M Dunham, Ann C Kelley, Jendrik Hentschel, Kenn Gerdes, V Ramakrishnan, Ditlev E Brodersen

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

134 citing papers in PubMed, 227 citations in OpenAlex.

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  13. Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025
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  19. Frontiers in microbiology · 2023
    Article
  20. Review

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

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 2 countries.

Cajetan NeubauerMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Yong-Gui Gao
Kasper R Andersen
Christine M Dunham
Ann C Kelley
Jendrik Hentschel
Kenn Gerdes
V Ramakrishnan
Ditlev E Brodersen
MRC Laboratory of Molecular Biology · GBAarhus University · DKNewcastle University · GB

Funding

Medical Research Council MC_U105184332Wellcome Trust
6 · The paper itself

Abstract

Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 A) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 A) and after (3.6 A) cleavage. RelE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2'-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in RelE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.

Indexed as

Bacterial ToxinsEscherichia coliEscherichia coli ProteinsModels, MolecularRibosomesRNA, MessengerRNA, Ribosomal, 16SThermus thermophilusBacterial ToxinsEscherichia coli ProteinsRelE protein, E coliRNA, MessengerRNA, Ribosomal, 16S

Identifiers

PMID20005802
PMCPMC2807027
OpenAlexW2022115313

What OpenQuestion holds

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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.