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Ribosomal Hibernation-Associated Factors in Escherichia coli

Bacteria convert active 70S ribosomes to inactive 100S ribosomes to survive under various stress conditions. This state, in which the ribosome loses its translational activity, is known as ribosomal hibernation. In gammaproteobacteria such as Escherichia coli, ribosome modulation factor and hibernat...

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Autores principales: Maki, Yasushi, Yoshida, Hideji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778775/
https://www.ncbi.nlm.nih.gov/pubmed/35056482
http://dx.doi.org/10.3390/microorganisms10010033
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author Maki, Yasushi
Yoshida, Hideji
author_facet Maki, Yasushi
Yoshida, Hideji
author_sort Maki, Yasushi
collection PubMed
description Bacteria convert active 70S ribosomes to inactive 100S ribosomes to survive under various stress conditions. This state, in which the ribosome loses its translational activity, is known as ribosomal hibernation. In gammaproteobacteria such as Escherichia coli, ribosome modulation factor and hibernation-promoting factor are involved in forming 100S ribosomes. The expression of ribosome modulation factor is regulated by (p)ppGpp (which is induced by amino acid starvation), cAMP-CRP (which is stimulated by reduced metabolic energy), and transcription factors involved in biofilm formation. This indicates that the formation of 100S ribosomes is an important strategy for bacterial survival under various stress conditions. In recent years, the structures of 100S ribosomes from various bacteria have been reported, enhancing our understanding of the 100S ribosome. Here, we present previous findings on the 100S ribosome and related proteins and describe the stress-response pathways involved in ribosomal hibernation.
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spelling pubmed-87787752022-01-22 Ribosomal Hibernation-Associated Factors in Escherichia coli Maki, Yasushi Yoshida, Hideji Microorganisms Review Bacteria convert active 70S ribosomes to inactive 100S ribosomes to survive under various stress conditions. This state, in which the ribosome loses its translational activity, is known as ribosomal hibernation. In gammaproteobacteria such as Escherichia coli, ribosome modulation factor and hibernation-promoting factor are involved in forming 100S ribosomes. The expression of ribosome modulation factor is regulated by (p)ppGpp (which is induced by amino acid starvation), cAMP-CRP (which is stimulated by reduced metabolic energy), and transcription factors involved in biofilm formation. This indicates that the formation of 100S ribosomes is an important strategy for bacterial survival under various stress conditions. In recent years, the structures of 100S ribosomes from various bacteria have been reported, enhancing our understanding of the 100S ribosome. Here, we present previous findings on the 100S ribosome and related proteins and describe the stress-response pathways involved in ribosomal hibernation. MDPI 2021-12-24 /pmc/articles/PMC8778775/ /pubmed/35056482 http://dx.doi.org/10.3390/microorganisms10010033 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Maki, Yasushi
Yoshida, Hideji
Ribosomal Hibernation-Associated Factors in Escherichia coli
title Ribosomal Hibernation-Associated Factors in Escherichia coli
title_full Ribosomal Hibernation-Associated Factors in Escherichia coli
title_fullStr Ribosomal Hibernation-Associated Factors in Escherichia coli
title_full_unstemmed Ribosomal Hibernation-Associated Factors in Escherichia coli
title_short Ribosomal Hibernation-Associated Factors in Escherichia coli
title_sort ribosomal hibernation-associated factors in escherichia coli
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778775/
https://www.ncbi.nlm.nih.gov/pubmed/35056482
http://dx.doi.org/10.3390/microorganisms10010033
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