Charging levels of four tRNA species in Escherichia coli Rel+ and Rel− strains during amino acid starvation: a simple model for the effect of ppGpp on translational accuracy11Edited by D. E. Draper

2001 ◽  
Vol 307 (3) ◽  
pp. 785-798 ◽  
Author(s):  
Michael A Sørensen
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Simple Model ◽  
Amino Acid Starvation ◽  
Trna Species

How Optimized Is the Translational Machinery in Escherichia coli, Salmonella typhimurium and Saccharomyces cerevisiae?

Genetics ◽  
1998 ◽  
Vol 149 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Xuhua Xia
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Salmonella Typhimurium ◽  
Codon Usage ◽  
Translational Efficiency ◽  
Square Root ◽  
Translational Machinery ◽  
Mutual Adaptation ◽  
Trna Species

Abstract The optimization of the translational machinery in cells requires the mutual adaptation of codon usage and tRNA concentration, and the adaptation of tRNA concentration to amino acid usage. Two predictions were derived based on a simple deterministic model of translation which assumes that elongation of the peptide chain is rate-limiting. The highest translational efficiency is achieved when the codon recognized by the most abundant tRNA reaches the maximum frequency. For each codon family, the tRNA concentration is optimally adapted to codon usage when the concentration of different tRNA species matches the square-root of the frequency of their corresponding synonymous codons. When tRNA concentration and codon usage are well adapted to each other, the optimal content of all tRNA species carrying the same amino acid should match the square-root of the frequency of the amino acid. These predictions are examined against empirical data from Escherichia coli, Salmonella typhimurium, and Saccharomyces cerevisiae.

Differential effect of amino acid starvation on polysome decay in escherichia coli

1978 ◽  
Vol 4 (1) ◽  
pp. 21-24 ◽  
Author(s):  
J. Roche ◽  
A. J. Cozzone ◽  
P. Donini ◽  
V. Santonastaso
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Differential Effect ◽  
Amino Acid Starvation

scholarly journals Regulation of Escherichia coli RelA Requires Oligomerization of the C-Terminal Domain

2001 ◽  
Vol 183 (2) ◽  
pp. 570-579 ◽  
Author(s):  
Michal Gropp ◽  
Yael Strausz ◽  
Miriam Gross ◽  
Gad Glaser
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Catalytic Domain ◽  
Mutational Analysis ◽  
Amino Acid Starvation ◽  
E Coli ◽  
Terminal Domain ◽  
Negative Effect ◽  
And Control ◽  
Two Hybrid

ABSTRACT The E. coli RelA protein is a ribosome-dependent (p)ppGpp synthetase that is activated in response to amino acid starvation. RelA can be dissected both functionally and physically into two domains: The N-terminal domain (NTD) (amino acids [aa] 1 to 455) contains the catalytic domain of RelA, and the C-terminal domain (CTD) (aa 455 to 744) is involved in regulating RelA activity. We used mutational analysis to localize sites important for RelA activity and control in these two domains. We inserted two separate mutations into the NTD, which resulted in mutated RelA proteins that were impaired in their ability to synthesize (p)ppGpp. When we caused the CTD inrelA + cells to be overexpressed, (p)ppGpp accumulation during amino acid starvation was negatively affected. Mutational analysis showed that Cys-612, Asp-637, and Cys-638, found in a conserved amino acid sequence (aa 612 to 638), are essential for this negative effect of the CTD. When mutations corresponding to these residues were inserted into the full-length relA gene, the mutated RelA proteins were impaired in their regulation. In attempting to clarify the mechanism through which the CTD regulates RelA activity, we found no evidence for competition for ribosomal binding between the normal RelA and the overexpressed CTD. Results from CyaA complementation experiments of the bacterial two-hybrid system fusion plasmids (G. Karimova, J. Pidoux, A. Ullmann, and D. Ladant, Proc. Natl. Acad. Sci. USA 95:5752–5756, 1998) indicated that the CTD (aa 564 to 744) is involved in RelA-RelA interactions. Our findings support a model in which RelA activation is regulated by its oligomerization state.

scholarly journals Multi-step resistance to Chloramphenicol in RC-stringent Escherichia coli K12—its effect on the induction of RNA synthesis by antibiotics under amino acid starvation

1965 ◽  
Vol 6 (2) ◽  
pp. 304-309 ◽  
Author(s):  
E. C. R. Reeve ◽  
J. O. Bishop
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Resistant Strain ◽  
Parent Strain ◽  
Rna Synthesis ◽  
Amino Acid Starvation ◽  
Sensitive Strain ◽  
Escherichia Coli K12 ◽  
High Doses

A multi-step Chloramphenicol (CM)-resistant derivative of an RC-stringent strain of Escherichia coli auxotrophic for threonine and leucine was resistant also to Aureomycin (AM) and Puromycin (PM). All three antibiotics released the repression of RNA synthesis due to amino acid starvation in the CM-sensitive parent strain, their relative activities being about 1:10:100 for AM: CM: PM. High doses of AM and CM failed to induce RNA synthesis. The CM-resistant strain required greater concentrations of each antibiotic than the sensitive strain to induce the same level of RNA synthesis, and appeared to be about one hundred times, ten times and five times more resistant to CM, AM and PM, respectively, than the sensitive strain.

Amino acid starvation in an Escherichia coli auxotroph

1960 ◽  
Vol 44 ◽  
pp. 491-500 ◽  
Author(s):  
Avram Goldstein ◽  
Beverly J. Brown
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Starvation

scholarly journals The global, ppGpp-mediated stringent response to amino acid starvation in Escherichia coli

2008 ◽  
Vol 68 (5) ◽  
pp. 1128-1148 ◽  
Author(s):  
Matthew F. Traxler ◽  
Sean M. Summers ◽  
Huyen-Tran Nguyen ◽  
Vineetha M. Zacharia ◽  
G. Aaron Hightower ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Stringent Response ◽  
Amino Acid Starvation
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