Abstract
Selenaproline is a proline analog having the C-4 methylene group substituted by a selenium atom. It has been demonstrated that selenaproline is activated and transferred to tRNA Pro by either Escherichia coli or rat liver aminoacyl-tRNA synthetases in competition with proline, and that it inhibits polypeptide synthesizing systems from E. coli, rat liver or rabbit reticulocytes. Analyzing the polysomal pattern of reticulocyte lysate it has been shown that selenaproline inhibits the ribosome run-off. Studying the effect of the addition of puromycin to the polypeptide synthesizing system, data have been obtained indicating that selenaproline may be incorporated in the growing polypeptide chain but impairs further chain elongation. All tests were performed in comparison with thiaproline, a proline analog having the C-4 methylene group substituted by a sulfur atom, which is known to act as a competitive inhibitor of proline. In all the reactions studied both thiaproline and selenaproline show similar inhibitory effects. The main difference between thiaproline and selenaproline is that the inhibitory effects of the latter are evident at lower concentrations and are not completely reverted by proline.
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