Expression of ribosome modulation factor (RMF) in Escherichia coli requires ppGpp

2001 ◽  
Vol 6 (8) ◽  
pp. 665-676 ◽  
Author(s):  
Kaori Izutsu ◽  
Akira Wada ◽  
Chieko Wada
Keyword(s):  
Escherichia Coli ◽  
Modulation Factor ◽  
Ribosome Modulation Factor

The Ribosome Modulation Factor (RMF) Binding Site on the 100S Ribosome of Escherichia coli

2002 ◽  
Vol 132 (6) ◽  
pp. 983-989 ◽  
Author(s):  
H. Yoshida ◽  
Y. Maki ◽  
H. Kato ◽  
H. Fujisawa ◽  
K. Izutsu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Modulation Factor ◽  
Ribosome Modulation Factor

scholarly journals Ribosomal Hibernation-Associated Factors in Escherichia coli

2021 ◽  
Vol 10 (1) ◽  
pp. 33
Author(s):  
Yasushi Maki ◽  
Hideji Yoshida
Keyword(s):  
Escherichia Coli ◽  
Biofilm Formation ◽  
Amino Acid Starvation ◽  
Stress Conditions ◽  
Metabolic Energy ◽  
Bacterial Survival ◽  
Modulation Factor ◽  
Translational Activity ◽  
Related Proteins ◽  
Ribosome Modulation Factor

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.

scholarly journals Modulation of mRNA Stability Participates in Stationary-Phase-Specific Expression of Ribosome Modulation Factor

2005 ◽  
Vol 187 (6) ◽  
pp. 1951-1958 ◽  
Author(s):  
Toshiko Aiso ◽  
Hideji Yoshida ◽  
Akira Wada ◽  
Reiko Ohki
Keyword(s):  
Stationary Phase ◽  
Growth Phase ◽  
Mrna Stability ◽  
De Novo ◽  
Fresh Medium ◽  
Specific Expression ◽  
Modulation Factor ◽  
Inactive Form ◽  
Regulation Of Growth ◽  
Ribosome Modulation Factor

ABSTRACT The expression of ribosome modulation factor (RMF) is induced during stationary phase in Escherichia coli. RMF participates in the dimerization of 70S ribosomes to form the 100S ribosome, which is the translationally inactive form of the ribosome. To elucidate the involvement of the control of mRNA stability in growth-phase-specific rmf expression, we investigated rmf mRNA stability in stationary-phase cells and cells inoculated into fresh medium. The rmf mRNA was found to have an extremely long half-life during stationary phase, whereas destabilization of this mRNA took place after the culture was inoculated into fresh medium. RMF and 100S ribosomes disappeared from cells 1 min after inoculation. In addition to control by ppGpp-dependent transcription, these results indicate that the modulation of rmf mRNA stability is also involved in the regulation of growth-phase-specific rmf expression. Unexpectedly, the postinoculation degradation of rmf mRNA was suppressed by the addition of rifampin, suggesting that de novo RNA synthesis is necessary for degradation. This degradation was also suppressed in both a poly(A) polymerase-deficient and an rne-131 mutant strain. We cloned and sequenced the 3′-proximal regions of rmf mRNAs and found that most of these 3′ ends terminated at the ρ-independent terminator with the addition of a one- to five-A oligo(A) tail in either stationary-phase or inoculated cells. No difference was observed in the length of the poly(A) tail between stationary-phase and inoculated cells. These results suggest that a certain postinoculation-specific regulatory factor participates in the destabilization of rmf mRNA and is dependent on polyadenylation.

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