Abstract
Abstract By means of a convenient method for separating phenylalanyl puromycin from diphenylalanyl puromycin, it was found that, upon reaction with puromycin, phenylalanyl transfer RNA bound to ribosomes at 5 to 6 mm Mg++ yields phenylalanyl puromycin exclusively while phenylalanyltRNA bound at 13 mm Mg++ yields diphenylalanyl puromycin as well as phenylalanyl puromycin. Tetracycline inhibited mostly the binding of phenylalanyl-tRNA to the acceptor site, but the binding to the donor site may be inhibited at 13 mm Mg++. Puromycin reaction of phenylalanyl-tRNA bound to the donor site was inhibited by the presence of N-acetylphenylalanyl-tRNA at the acceptor site.
Highlights
We extended our studies on the ribosomal sites with the method which separates phenylalanyl puromycin from diphenylalanyl puromycin to elucidate the action of tetracycline and puromycin
Escherickia co& Extract and Other hlaterials-Preparation of ribosomes, tRNA from E. coli B, and aminoacyl-tRNA have been described in the previous communications [1]
Preceding reports on the action of protein synthesis inhibitor [9] were based on the assumption that in the presence of low Mg++, binding of phenylalanyl-tRNA to ribosomes took place mostly to the donor site while both donor and acceptor sites were occupied with phenylalanyl-tRNA in the presence of high Mg+f
Summary
Escherickia co& Extract and Other hlaterials-Preparation of ribosomes, tRNA from E. coli B, and aminoacyl-tRNA have been described in the previous communications [1]. A typical binding reaction mixture (0.5 ml) for the isolation of the complex, unless otherwise specified, contained 50 mM Tris-HCl (pH 7.2), 6 mM magnesium acetate, 40 mM ammonium chloride, 400 pg of poly(U), 5.2 mg of tRNA containing 8.5 X lo cpm of [14C]phenylalanyl-tRNA, and 5.8 mg of ribosomes. This binding condition was called condition A. The binding reaction was performed under identical conditions except that the Mg+f concentration was 13 mM
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