A Comprehensive Review of Ribosomal Hibernation and Associated Factors in Escherichia coli | Chapter 3 | Microbiology and Biotechnology Research: An Overview Vol. 1

Bacteria have developed sophisticated adaptive systems to survive during various environmental changes, including nutrient starvation, temperature shock, osmolarity changes, and rapid pH changes. Bacteria convert active 70S ribosomes to inactive 100S ribosomes to survive under various stress conditions. Recently, high-resolution structures of 100S ribosomes from various bacteria have been reported, improving the understanding of ribosome hibernation. In this review, previous findings on the 100S ribosome and related protein factors in E. coli are described. This study is an attempt to integrate the hibernation stage into the ribosome cycle and discuss the elaborate stress response pathway involved in bacterial translational control. The state, in which the ribosome loses its translational activity, is known as ribosomal hibernation. In gammaproteobacteria such as Escherichia coli, ribosome modulation factor (RMF) and hibernation-promoting factor (HPF) 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 and depletion of metal-ions. (p)ppGpp regulates transcriptional activity and decreases ribosome biosynthesis for environmental adaptation by interacting with RNA polymerase. This indicates that the formation of 100S ribosomes is an important strategy for bacterial survival under various stress conditions. The genes for the ribosomal hibernation factors are scattered throughout the E. coli genome and use different expression pathways. Therefore, determining the expression mechanism of protein factors, such as RMF and HPF, which contribute to the formation of 100S ribosomes, will be useful for considering the effective use of antibiotics.

 

Author (s) Details

 

Yasushi Maki
Department of Physics, Osaka Medical and Pharmaceutical University, Takatsuki 569-8686, Japan.

 

Hideji YoshidaA
Department of Physics, Osaka Medical and Pharmaceutical University, Takatsuki 569-8686, Japan.

 

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