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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Shared Science Publishers OG
2020
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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. |
format | Online Article Text |
id | pubmed-7199280 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Shared Science Publishers OG |
record_format | MEDLINE/PubMed |
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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