Evidence map›Paper›PMID 23475961›Full record

ArticleGenes & development2013

Targeted decay of a regulatory small RNA by an adaptor protein for RNase E and counteraction by an anti-adaptor RNA.

Yvonne Göpel, Kai Papenfort, Birte Reichenbach, Jörg Vogel, Boris Görke

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
–field-weighted citation impact
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

84 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026
    Review
  3. Review
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  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Food for Thought: Proteomics for Meat Safety.Life (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Article
  16. Key players in regulatory RNA realm of bacteria.Biochemistry and biophysics reports · 2022
    Review
  17. Review
  18. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
  19. Article
  20. Article

24 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

5 authors at 2 institutions in 1 country.

Yvonne GöpelDepartment of General Microbiology, Institute of Microbiology and Genetics, Georg-August-University, D-37077 Göttingen, Germany.
Kai Papenfort
Birte Reichenbach
Jörg Vogel
Boris Görke
University of Göttingen · DEUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial small RNAs (sRNAs) are well established to regulate diverse cellular processes, but how they themselves are regulated is less understood. Recently, we identified a regulatory circuit wherein the GlmY and GlmZ sRNAs of Escherichia coli act hierarchically to activate mRNA glmS, which encodes glucosamine-6-phosphate (GlcN6P) synthase. Although the two sRNAs are highly similar, only GlmZ is a direct activator that base-pairs with the glmS mRNA, aided by protein Hfq. GlmY, however, does not bind Hfq and activates glmS indirectly by protecting GlmZ from RNA cleavage. This complex regulation feedback controls the levels of GlmS protein in response to its product, GlcN6P, a key metabolite in cell wall biosynthesis. Here, we reveal the molecular basis for the regulated turnover of GlmZ, identifying RapZ (RNase adaptor protein for sRNA GlmZ; formerly YhbJ) as a novel type of RNA-binding protein that recruits the major endoribonuclease RNase E to GlmZ. This involves direct interaction of RapZ with the catalytic domain of RNase E. GlmY binds RapZ through a secondary structure shared by both sRNAs and therefore acts by molecular mimicry as a specific decoy for RapZ. Thus, in analogy to regulated proteolysis, RapZ is an adaptor, and GlmY is an anti-adaptor in regulated turnover of a regulatory small RNA.

Indexed as

RNA StabilityAmino Acid SequenceEndoribonucleasesEscherichia coliEscherichia coli ProteinsMolecular MimicryMolecular Sequence DataProtein BindingProtein Structure, TertiaryRNA, BacterialRNA-Binding ProteinsSequence AlignmentEndoribonucleasesEscherichia coli Proteinsribonuclease ERNA, BacterialRNA-Binding ProteinsYhbJ protein, E coli

Identifiers

PMID23475961
PMCPMC3605468
OpenAlexW2149483164

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.