Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. the interaction of cholesteryl 14-methylhexadecanoate.
1. Transferase I from rat liver extracted with iso-octane binds significantly less aminoacyl-tRNA than the non-extracted enzyme. The original activity can be fully restored by the addition of cholesteryl 14-methylhexadecanoate. The binding capacity for GTP is not affected by the extraction. 2. In the presence of extracted transferase I the binding of aminoacyl-tRNA to ribosomes is decreased to 11-26% and the simultaneous binding of GTP to 32-43%. Cholesteryl 14-methylhexadecanoate induces a full reactivation of the extracted enzyme in both respects. 3. Extracted complexes A (aminoacyl-tRNA-GTP-transferase I) become bound to ribosomes to the same extent as the corresponding non-extracted preparations. 4. It is concluded that cholesteryl 14-methylhexadecanoate interacts with the binding site of transferase I for aminoacyl-tRNA and secondarily with that for GTP. It does not affect the binding site for ribosomes.
D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D006160:Guanosine Triphosphate; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology; D010759:Phosphorus Isotopes; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D051381:Rats; D012270:Ribosomes / Q000378:metabolism*; D013261:Sterols; D014166:Transferases / Q000378:metabolism
D000596:Amino Acids; D010759:Phosphorus Isotopes; D013261:Sterols; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D014166:Transferases