Cysteine homeostasis under inhibition of protein synthesis in Escherichia coli cells

Amino Acids ◽  
2019 ◽  
Vol 51 (10-12) ◽  
pp. 1577-1592 ◽  
Author(s):  
Galina V. Smirnova ◽  
Aleksey V. Tyulenev ◽  
Kseniya V. Bezmaternykh ◽  
Nadezda G. Muzyka ◽  
Vadim Y. Ushakov ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Escherichia Coli Cells ◽  
Inhibition Of Protein Synthesis

scholarly journals Lethal Action of Quinolones against a Temperature-Sensitive dnaB Replication Mutant of Escherichia coli

2006 ◽  
Vol 50 (1) ◽  
pp. 362-364 ◽  
Author(s):  
Xilin Zhao ◽  
Muhammad Malik ◽  
Nymph Chan ◽  
Alex Drlica-Wagner ◽  
Jian-Ying Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Dna Replication ◽  
Nalidixic Acid ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Lethal Action ◽  
Inhibition Of Protein Synthesis

ABSTRACT Inhibition of DNA replication in an Escherichia coli dnaB-22 mutant failed to block quinolone-mediated lethality. Inhibition of protein synthesis by chloramphenicol inhibited nalidixic acid lethality and, to a lesser extent, ciprofloxacin lethality in both dnaB-22 and wild-type cells. Thus, major features of quinolone-mediated lethality do not depend on ongoing replication.

scholarly journals The action of streptomycin in a mutant of Escherichia coli with increased sensitivity to the antibiotic

1970 ◽  
Vol 118 (4) ◽  
pp. 659-666 ◽  
Author(s):  
G. Turnock
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Normal Cell ◽  
Permeability Barrier ◽  
Bactericidal Action ◽  
Site Of Action ◽  
Inhibition Of Protein Synthesis ◽  
Increased Sensitivity ◽  
Lag Period

A mutant of Escherichia coli with increased sensitivity to streptomycin has been studied. This strain differed from a normal strs strain in that streptomycin produced inhibition of protein synthesis and loss of viability with almost no lag period. Chloramphenicol protected a normal strs strain but not the mutant against the bactericidal action of streptomycin. The results obtained support the idea that access of streptomycin to its site of action in a normal cell is restricted, and that this restriction, which is much less effective in the mutant, probably involves a permeability barrier. Comparison of the inhibition of protein synthesis by streptomycin with concomitant changes in the distribution of polyribosomes in both strains suggested that the antibiotic can directly inhibit the translation of mRNA.

Metabolic fate of initiation factors after inhibition of protein synthesis in Escherichia coli

1973 ◽  
Vol 125 (4) ◽  
pp. 301-318 ◽  
Author(s):  
Lucienne Legault-Demare ◽  
Claude Jeantet ◽  
François Gros
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Metabolic Fate ◽  
Initiation Factors ◽  
Inhibition Of Protein Synthesis

scholarly journals Properties of a Revertant of Escherichia coli Viable in the Presence of Spermidine Accumulation: Increase in l-Glycerol 3-Phosphate

2001 ◽  
Vol 183 (15) ◽  
pp. 4493-4498 ◽  
Author(s):  
V. Samuel Raj ◽  
Hideyuki Tomitori ◽  
Madoka Yoshida ◽  
Auayporn Apirakaramwong ◽  
Keiko Kashiwagi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Death ◽  
Protein Synthesis ◽  
Glycerol Kinase ◽  
High Concentration ◽  
Gene Encoding ◽  
E Coli ◽  
Inhibition Of Protein Synthesis ◽  
High Concentrations ◽  
Ribosome Modulation Factor

ABSTRACT Escherichia coli CAG2242 cells are deficient in thespeG gene encoding spermidine acetyltransferase. When these cells were cultured in the presence of 0.5 to 4 mM spermidine, their viability was greatly decreased through the inhibition of protein synthesis by overaccumulation of spermidine. When the cells were cultured with a high concentration of spermidine (4 mM), a revertant strain was obtained. We found that a 55-kDa protein, glycerol kinase, was overexpressed in the revertant and that synthesis of a ribosome modulation factor and the RNA polymerase ς38 subunit, factors important for cell viability, was increased in the revertant. Levels of l-glycerol 3-phosphate also increased in the revertant. Transformation of glpFK, which encodes a glycerol diffusion facilitator (glpF) and glycerol kinase (glpK), to E. coli CAG2242 partially prevented the cell death caused by accumulation of spermidine. It was also found that l-glycerol 3-phosphate inhibited spermidine binding to ribosomes and attenuated the inhibition of protein synthesis caused by high concentrations of spermidine. These results indicate that l-glycerol 3-phosphate reduces the binding of excess amounts of spermidine to ribosomes so that protein synthesis is recovered.

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