The effect of guanosine nucleotides on the multiple forms of protein synthesis elongation factor 1 from wheat embryos

1973 ◽  
Vol 159 (1) ◽  
pp. 353-361 ◽  
Author(s):  
Adela Tarragó ◽  
Jorge E. Allende ◽  
Betty Redfield ◽  
Herbert Weissbach
1987 ◽  
Vol 244 (2) ◽  
pp. 287-294 ◽  
Author(s):  
T G Obrig ◽  
T P Moran ◽  
J E Brown

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.


1973 ◽  
pp. 61-70
Author(s):  
Simon Litvak ◽  
Adela Tarrago ◽  
Beatriz Levy ◽  
Lucia Manzocchi ◽  
Marta Gatica ◽  
...  

1973 ◽  
Vol 70 (12) ◽  
pp. 3282-3286 ◽  
Author(s):  
H.-M. Moon ◽  
B. Redfield ◽  
S. Millard ◽  
F. Vane ◽  
H. Weissbach

1974 ◽  
Vol 71 (6) ◽  
pp. 2179-2182 ◽  
Author(s):  
A. B. Legocki ◽  
B. Redfield ◽  
C. K. Liu ◽  
H. Weissbach

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