scholarly journals Structure and probable genetic location of a "ribosome modulation factor" associated with 100S ribosomes in stationary-phase Escherichia coli cells.

1990 ◽  
Vol 87 (7) ◽  
pp. 2657-2661 ◽  
Author(s):  
A. Wada ◽  
Y. Yamazaki ◽  
N. Fujita ◽  
A. Ishihama
Keyword(s):  
Escherichia Coli ◽  
Stationary Phase ◽  
Genetic Location ◽  
Modulation Factor ◽  
Escherichia Coli Cells ◽  
Ribosome Modulation Factor

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.

SlyD-dependent nickel delivery limits maturation of [NiFe]-hydrogenases in late-stationary phase Escherichia coli cells

Metallomics ◽  
2015 ◽  
Vol 7 (4) ◽  
pp. 683-690 ◽  
Author(s):  
Constanze Pinske ◽  
Frank Sargent ◽  
R. Gary Sawers
Keyword(s):  
Escherichia Coli ◽  
Stationary Phase ◽  
Late Stationary Phase ◽  
E Coli ◽  
Escherichia Coli Cells

The metallochaperone SlyD is essential for nickel delivery to hydrogenase in stationary phaseE. colicells.

scholarly journals Nucleoids Dynamic in Escherichia coli: A Growth Phase Dependent Process

1970 ◽  
Vol 23 (2) ◽  
pp. 81-88 ◽  
Author(s):  
Ali Azam Talukder ◽  
M Anwar Hossain ◽  
Mamoru Yamada ◽  
Akira Ishihama
Keyword(s):  
Escherichia Coli ◽  
Stationary Phase ◽  
Gene Silencing ◽  
Cell Survival ◽  
Growth Phase ◽  
Genomic Dna ◽  
Bacterial Dna ◽  
Escherichia Coli Cells ◽  
Dna Organization ◽  
Nucleoid Proteins

Bacterial DNA compacts in nucleoid bodies. The organization of nucleoid body depends on the association of genomic DNA with a numbers of histone-like proteins. The relax nucleoids organization in rapidly growing Escherichia coli cells associate with six major proteins, Fis, HU, Hfq, H-NS, StpA and IHF, but at stationary phase the nucleoids further tightly pack with Dps. The final steps of compact nucleoids formation occurs with association of MukBEF complex - a bacterial condensin. The change of nucleoid proteins composition in stationary phase accompanies compact DNA organization and genes silencing. Thus, compact nucleoid organization and gene silencing may be crucial for cell survival in stationary phase.Keywords: Escherichia coli, Nucleoid body, Nucleoid proteins, Nucleoid compaction, CondensinDOI: http://dx.doi.org/10.3329/bjm.v23i2.867 Bangladesh J Microbiol, Volume 23, Number 2, December 2006, pp 81-88

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

Involvement of ppGpp, Ribosome Modulation Factor, and Stationary Phase-Specific Sigma Factor ςS in the Decrease in Cell Viability Caused by Spermidine

1999 ◽  
Vol 264 (3) ◽  
pp. 643-647 ◽  
Author(s):  
Auayporn Apirakaramwong ◽  
Keiko Kashiwagi ◽  
V.Samuel Raj ◽  
Kaori Sakata ◽  
Yoshimi Kakinuma ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Cell Viability ◽  
Sigma Factor ◽  
Modulation Factor ◽  
Ribosome Modulation Factor
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