Evidence map›Paper›PMID 32065419›Full record

ArticleThe EMBO journal2020

Small RNA-binding protein RapZ mediates cell envelope precursor sensing and signaling in Escherichia coli.

Muna A Khan, Svetlana Durica-Mitic, Yvonne Göpel, Ralf Heermann, Boris Görke

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. What makes a small RNA work?Nucleic acids research · 2025
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Small RNA GcvB Regulates Oxidative Stress Response ofAntioxidants (Basel, Switzerland) · 2021
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Muna A KhanDepartment of Microbiology, Immunobiology and Genetics, Max Perutz Labs, Vienna Biocenter (VBC), University of Vienna, Vienna, Austria.
Svetlana Durica-MiticDepartment of Microbiology, Immunobiology and Genetics, Max Perutz Labs, Vienna Biocenter (VBC), University of Vienna, Vienna, Austria.
Yvonne GöpelDepartment of Microbiology, Immunobiology and Genetics, Max Perutz Labs, Vienna Biocenter (VBC), University of Vienna, Vienna, Austria.
Ralf HeermannMicrobiology and Wine Research, Institute for Molecular Physiology, Johannes Gutenberg-University Mainz, Mainz, Germany.
Boris GörkeDepartment of Microbiology, Immunobiology and Genetics, Max Perutz Labs, Vienna Biocenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0002-1682-5387
University of Vienna · ATJohannes Gutenberg University Mainz · DE

Funding

Austrian Science Fund (FWF) Doktoratskolleg W1207-B09Austrian Science Fund (FWF) P26681-B22Austrian Science Fund (FWF) P32410-BAustrian Science Fund FWF P 26681Austrian Science Fund FWF P 32410
6 · The paper itself

Abstract

The RNA-binding protein RapZ cooperates with small RNAs (sRNAs) GlmY and GlmZ to regulate the glmS mRNA in Escherichia coli. Enzyme GlmS synthesizes glucosamine-6-phosphate (GlcN6P), initiating cell envelope biosynthesis. GlmZ activates glmS expression by base-pairing. When GlcN6P is ample, GlmZ is bound by RapZ and degraded through ribonuclease recruitment. Upon GlcN6P depletion, the decoy sRNA GlmY accumulates through a previously unknown mechanism and sequesters RapZ, suppressing GlmZ decay. This circuit ensures GlcN6P homeostasis and thereby envelope integrity. In this work, we identify RapZ as GlcN6P receptor. GlcN6P-free RapZ stimulates phosphorylation of the two-component system QseE/QseF by interaction, which in turn activates glmY expression. Elevated GlmY levels sequester RapZ into stable complexes, which prevents GlmZ decay, promoting glmS expression. Binding of GlmY also prevents RapZ from activating QseE/QseF, generating a negative feedback loop limiting the response. When GlcN6P is replenished, GlmY is released from RapZ and rapidly degraded. We reveal a multifunctional sRNA-binding protein that dynamically engages into higher-order complexes for metabolite signaling.

Indexed as

Signal TransductionBacterial ProteinsDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGlucosamineGlucose-6-PhosphateGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)Receptors, AdrenergicRNA, BacterialRNA-Binding ProteinsRNA, MessengerRNA, Small UntranslatedBacterial Proteinscomponent S, glutamate mutase protein, BacteriaDNA-Binding ProteinsEscherichia coli ProteinsGlucosamineglucosamine 6-phosphateGlucose-6-PhosphateGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)QseE protein, E coliQseF protein, E coliReceptors, AdrenergicRNA, BacterialRNA-Binding ProteinsRNA, MessengerRNA, Small UntranslatedYhbJ protein, E colicell envelope precursor glucosamine-6-phosphatenegative feedback loopRNA-binding protein RapZsmall RNAs GlmY and GlmZtwo-component system QseE-QseF

Identifiers

PMID32065419
PMCPMC7073468
OpenAlexW3005766797

What Socratic 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 Socratic graph.