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A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria

Synthesis of glucosamine-6-phosphate (GlcN6P) by the enzyme GlmS initiates bacterial cell envelope biosynthesis. To ensure ongoing synthesis, GlcN6P homeostasis is required. Escherichia coli achieves this through a post-transcriptional control mechanism comprising the RNA-binding protein RapZ and sm...

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Autores principales: Khan, Muna A., Görke, Boris
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Shared Science Publishers OG 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7199280/
https://www.ncbi.nlm.nih.gov/pubmed/32391395
http://dx.doi.org/10.15698/mic2020.05.717
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author Khan, Muna A.
Görke, Boris
author_facet Khan, Muna A.
Görke, Boris
author_sort Khan, Muna A.
collection PubMed
description Synthesis of glucosamine-6-phosphate (GlcN6P) by the enzyme GlmS initiates bacterial cell envelope biosynthesis. To ensure ongoing synthesis, GlcN6P homeostasis is required. Escherichia coli achieves this through a post-transcriptional control mechanism comprising the RNA-binding protein RapZ and small RNAs (sRNAs) GlmY and GlmZ. GlmZ stimulates glmS translation by base-pairing. When GlcN6P is abundant, GlmZ is cleaved and inactivated by endoribonuclease RNase E. Cleavage depends on RapZ, which binds GlmZ and recruits RNase E. Decreasing GlcN6P concentrations provoke up-regulation of the decoy sRNA GlmY which sequesters RapZ, thereby suppressing GlmZ decay. In our current study we identify RapZ as the GlcN6P sensor. GlcN6P-free RapZ interacts with and stimulates phosphorylation of the two-component system (TCS) QseE/QseF triggering glmY expression. Thereby generated GlmY sequesters RapZ into stable complexes, allowing for glmS expression. Sequestration by GlmY also disables RapZ to stimulate QseE/QseF, providing a negative feed-back loop limiting the response. When GlcN6P is replenished, GlmY is released from RapZ and rapidly degraded. Our work has revealed a complex regulatory scenario, in which an RNA binding protein senses a metabolite and communicates with two sRNAs, a TCS and ribonuclease RNase E to achieve metabolite homeostasis.
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spelling pubmed-71992802020-05-08 A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria Khan, Muna A. Görke, Boris Microb Cell Microreview Synthesis of glucosamine-6-phosphate (GlcN6P) by the enzyme GlmS initiates bacterial cell envelope biosynthesis. To ensure ongoing synthesis, GlcN6P homeostasis is required. Escherichia coli achieves this through a post-transcriptional control mechanism comprising the RNA-binding protein RapZ and small RNAs (sRNAs) GlmY and GlmZ. GlmZ stimulates glmS translation by base-pairing. When GlcN6P is abundant, GlmZ is cleaved and inactivated by endoribonuclease RNase E. Cleavage depends on RapZ, which binds GlmZ and recruits RNase E. Decreasing GlcN6P concentrations provoke up-regulation of the decoy sRNA GlmY which sequesters RapZ, thereby suppressing GlmZ decay. In our current study we identify RapZ as the GlcN6P sensor. GlcN6P-free RapZ interacts with and stimulates phosphorylation of the two-component system (TCS) QseE/QseF triggering glmY expression. Thereby generated GlmY sequesters RapZ into stable complexes, allowing for glmS expression. Sequestration by GlmY also disables RapZ to stimulate QseE/QseF, providing a negative feed-back loop limiting the response. When GlcN6P is replenished, GlmY is released from RapZ and rapidly degraded. Our work has revealed a complex regulatory scenario, in which an RNA binding protein senses a metabolite and communicates with two sRNAs, a TCS and ribonuclease RNase E to achieve metabolite homeostasis. Shared Science Publishers OG 2020-04-15 /pmc/articles/PMC7199280/ /pubmed/32391395 http://dx.doi.org/10.15698/mic2020.05.717 Text en Copyright: © 2020 Khan and Görke https://creativecommons.org/licenses/by/4.0/ This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
spellingShingle Microreview
Khan, Muna A.
Görke, Boris
A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria
title A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria
title_full A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria
title_fullStr A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria
title_full_unstemmed A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria
title_short A multifunctional small RNA binding protein for sensing and signaling cell envelope precursor availability in bacteria
title_sort multifunctional small rna binding protein for sensing and signaling cell envelope precursor availability in bacteria
topic Microreview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7199280/
https://www.ncbi.nlm.nih.gov/pubmed/32391395
http://dx.doi.org/10.15698/mic2020.05.717
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