Stimulation of peptide elongation by thyroxine.
This study suggests that thyroxine stimulates peptide elongation in a cell-free rat liver polyribosome system. The thyroxine effect persists in the presence of sufficient aurintricarboxylic acid to prevent polyuridylic acid-stimulated peptide initiation. In addition, thyroxine stimulates elongation of pre-existing polyphenylalanine chains providing conclusive evidence that the effect does not depend on peptide initiation. Thyroxine does not stimulate release of nascent peptides from ribosomes into the supernatant phase of the reaction mixture. Therefore in this protein-synthesis system the thyroxine effect is expected to occur at one or more of the reactions of peptide chain elongation, which include aminoacyl-tRNA binding, peptide bond synthesis and translocation.
D000818:Animals; D001312:Aurintricarboxylic Acid / Q000494:pharmacology; D008099:Liver / Q000378:metabolism; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects*; D010455:Peptides / Q000378:metabolism; D011072:Poly U / Q000494:pharmacology; D051381:Rats; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism; D013974:Thyroxine / Q000494:pharmacology*; D014633:Valine / Q000378:metabolism
D010455:Peptides; D011072:Poly U; D001312:Aurintricarboxylic Acid; D014633:Valine; D013974:Thyroxine