6533b838fe1ef96bd12a5054
RESEARCH PRODUCT
Small RNA‐binding protein RapZ mediates cell envelope precursor sensing and signaling in Escherichia coli
Muna A. KhanYvonne GöpelBoris GörkeRalf HeermannSvetlana Durica-miticsubject
Small RNAsmall regulatory RNAcell envelope precursor glucosamine‐6‐phosphatemedicine.disease_causenegative feedback loopmetabolite sensing0302 clinical medicinetwo-component system QseE-QseFRNA-binding protein RapZRNA‐binding protein RapZGlucosamine0303 health sciencesbiologyEscherichia coli ProteinsGeneral NeuroscienceRNA-Binding ProteinsArticlesRNA BiologyMicrobiology Virology & Host Pathogen InteractionReceptors AdrenergicCell biologyDNA-Binding ProteinsRNA BacterialTransfer RNAPhosphorylationCell envelopeSignal TransductionGlucose-6-PhosphateGeneral Biochemistry Genetics and Molecular BiologyArticletwo‐component system QseE‐QseF03 medical and health sciencesBacterial Proteinscell envelope precursorEscherichia colimedicineRNA MessengerRibonucleaseMolecular BiologyEscherichia coli030304 developmental biologyMessenger RNAGeneral Immunology and MicrobiologyBinding proteinsmall RNAs GlmY and GlmZGene Expression Regulation BacterialMicroreviewRNA binding proteincell envelope precursor glucosamine-6-phosphatetwo-component systembiology.proteinRNA Small Untranslated030217 neurology & neurosurgerydescription
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.
year | journal | country | edition | language |
---|---|---|---|---|
2019-10-28 | The EMBO Journal |