Inhibition of amino acid incorporation in a cell-free system and inhibition of protein synthesis in cultured cells by reaction products of selenite and thiols

1983 ◽  
Vol 739 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Leendert N. Vernie ◽  
Martha De Vries ◽  
Leendert Karreman ◽  
Randolf J. Topp ◽  
Willy S. Bont
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Cultured Cells ◽  
Reaction Products ◽  
Amino Acid Incorporation ◽  
Free System ◽  
Cell Free System ◽  
Acid Incorporation ◽  
Inhibition Of Protein Synthesis ◽  
A Cell

scholarly journals Studies on the inhibition of protein synthesis by selenodiglutathione

1979 ◽  
Vol 180 (1) ◽  
pp. 213-218 ◽  
Author(s):  
L N Vernie ◽  
J G Collard ◽  
A P Eker ◽  
A de Wildt ◽  
I T Wilders
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Elongation Factor ◽  
Amino Acid Incorporation ◽  
Free System ◽  
Cell Free System ◽  
E Coli ◽  
Acid Incorporation ◽  
F Cells ◽  
A Cell

Amino acid incorporation in a cell-free system derived from rat liver has previously been found to be inhibited by GSSeSG (selenodiglutathione). In the present experiments the effect of GSSeSG on protein synthesis in 3T3-f cells, on growth and protein synthesis in Escherichia coli, and on amino acid incorporation in a cell-free system derived from E. coli, was studied. GSSeSG inhibits the incorporation of [3H]leucine into protein by 3T3-f cells. This inhibition cannot be reversed by removing GSSeSG and is correlated with the uptake of GSSeSG. Sodium selenite (Na2SeO3) and oxidized glutathione had no inhibitory effect in this system. [3H]Uridine or [3H]thymidine incorporation into RNA or DNA was not inhibited, indicating that the primary action of GSSeSG was on protein synthesis. GSSeSG did not influence the growth of E. coli in a synthetic medium, although enhanced amino acid incorporation was observed. In the cell-free system derived from E. coli, amino acid incorporation was not changed by GSSeSG, indicating that elongation factor G, in contrast to elongation factor 2 of mammalian cell systems, is not blocked by GSSeSG.

Suppressors suaC 109 and suaA 101 of Aspergillus nidulans alter the ribosomal phenotype in vitro

1987 ◽  
Vol 7 (12) ◽  
pp. 941-948 ◽  
Author(s):  
A. Zamir ◽  
S. S. Martinelli
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Ribosomal Proteins ◽  
Amino Acid Incorporation ◽  
Free System ◽  
Cell Free System ◽  
Translation Factors ◽  
Acid Incorporation

A new homologous, cell-free system for protein synthesis has been devised for use with ribosomes and elongation factors from Aspergillus nidulans. Ribosome preparations from strains with either the suaAlO1 or suaCl09 mutations have a higher misreading ratio (non-cognate:cognate amino acid incorporation) in the presence of hygromycin than controls. They can be classed as fidelity mutants. These results also prove that the mutations must be in genes coding for ribosomal proteins or enzymes which modify ribosomal proteins post-translationally. Alternatively, the genes could code for translation factors.

Amino acid incorporation by fig fruit ribosomes in a cell-free system

1972 ◽  
Vol 11 (2) ◽  
pp. 529-533 ◽  
Author(s):  
Nasr Marei ◽  
Ahmed I. Gadallah ◽  
Wendell W. Kilgore
Keyword(s):  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Free System ◽  
Cell Free System ◽  
Acid Incorporation ◽  
A Cell
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