Studies on the inhibition of protein synthesis by selenodiglutathione

Publisher Website
Google Scholar
Abstract
Amino acid incorporation in a cell-free system derived from rat liver was previously found to be inhibited by GSSeSG (selenodiglutathione). In the present experiments the effect of GSSeSG on protein synthesis in [mouse fibroblast] 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 incorpation 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, unlike elongation factor 2 of mammalian cell systems, is not blocked by GSSeSG.