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Molecular Pharmacology, Vol 9, 229-236, Copyright © 1973 by the American Society for Pharmacology and Experimental Therapeutics

Increased Binding of Transfer Ribonucleic Acid Species to Ribosomes under Conditions Interfering with Their Aminoacylation

KENNETH BALKOW 1 and MARCO RABINOVITZ 1

1 Laboratory of Physiology, National Cancer Institute, Bethesda, Maryland 20014

The agr-amino alcohols, histidinol and valinol, inhibited protein synthesis in the rabbit reticulocyte cell-free system by interfering with activation of histidine and valine, respectively. The lower rate of translation resulted in an increase in the polyribosome component of such systems. Histidinol promoted an accumulation of tRNAHis associated with ribosomes, and a similar result was found with valinol. The data indicate that deacylated tRNA is bound to ribosomes in a protein-synthesizing system when the acylated form is unavailable.

Submitted on November 2, 1972






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