Abstract
A reaction stimulated by elongation factor 2 (EF-2) is necessary for the formation of the initial peptide-bond in poly(U)-directed peptide synthesis on yeast ribosomal subunits. The stimulation is inhibited by fusidic acid or diphtheria toxin together with NAD. It is assumed that the reaction of EF-2 represents translocation: in the presence of EF-2 almost twice the amount of N-acetyl-phenylalanyl-tRNA is bound to ribosomes and moreover, upon addition of puromycin a considerable stimulation of N-acetyl-phenylalanyl-puromycin formation is found. Contradictory data in the literature on this subject may be due to nonenzymatic translocation caused by a high monovalent cation concentration in the ribosome preparations or to an unspecific method for the extraction of N-acetyl-phenylalanyl-puromycin.
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Pranger, M.H., Roos, M.H., Van Der Zeijst, B.A.M. et al. Requirements for the initiation of polyphenylalanine synthesis by recombined ribosomal subunits from yeast. Mol Biol Rep 1, 321–327 (1974). https://doi.org/10.1007/BF00309565
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DOI: https://doi.org/10.1007/BF00309565