scholarly journals Stimulation of Protein Synthesis in the Mitochondria of Sea Urchin Embryos before Gastrulation. (protein synthesis/sea urchin embryo/mitochondria/peptide elongation factor/mitosol)

1988 ◽  
Vol 30 (2) ◽  
pp. 137-145 ◽  
Author(s):  
TSUYOSHI KAWASHIMA ◽  
TOHRU NAKAZAWA
Keyword(s):  
Protein Synthesis ◽  
Sea Urchin ◽  
Elongation Factor ◽  
Sea Urchin Embryos ◽  
Sea Urchin Embryo ◽  
Peptide Elongation ◽  
Stimulation Of

Patterns and rates of protein synthesis in sea urchin embryos

1970 ◽  
Vol 21 (1-2) ◽  
pp. 105-124 ◽  
Author(s):  
Barry J. Fry ◽  
Paul R. Gross
Keyword(s):  
Protein Synthesis ◽  
Sea Urchin ◽  
Sea Urchin Embryos

scholarly journals The mode of action of Shiga toxin on peptide elongation of eukaryotic protein synthesis

1987 ◽  
Vol 244 (2) ◽  
pp. 287-294 ◽  
Author(s):  
T G Obrig ◽  
T P Moran ◽  
J E Brown
Keyword(s):  
Protein Synthesis ◽  
Complex Formation ◽  
Shiga Toxin ◽  
Mode Of Action ◽  
Elongation Factor ◽  
Shigella Dysenteriae ◽  
Gtpase Activity ◽  
Elongation Factor 2 ◽  
Peptide Elongation ◽  
Elongation Factor 1

The effect of Shiga toxin, from Shigella dysenteriae 1, on the component reactions of peptide elongation were investigated. Enzymic binding of [3H]phenylalanine-tRNA to reticulocyte ribosomes was inhibited by 50% at 7 nM toxin. Elongation factor 1 (eEF-1)-dependent GTPase activity was also inhibited. Both reactions were not restored by addition of excess eEF-1 protein. In contrast, toxin concentrations of 200 nM were required to inhibit by 50% the elongation factor 2 (eEF-2)-dependent translocation of aminoacyl-tRNA on ribosomes. Addition of excess eEF-2 restored translocation activity. The eEF-2-dependent GTPase activity was unaffected at toxin concentrations below 100 nM, and Shiga-toxin concentrations of up to 1,000 nM did not affect either GTP.eEF-2.ribosome complex-formation or peptidyltransferase activity. Thus Shiga toxin closely resembles alpha-sarcin in action, both being primary inhibitors of eEF-1-dependent reactions. In contrast, the 60 S ribosome inactivators ricin and phytolaccin are primary inhibitors of eEF-2-dependent reactions of peptide elongation.

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