title: Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. Formation and properties of an aminoacyl-transfer ribonucleic acid-transferase I complex.
abstract: 1. Transferase I of rat liver binds aminoacyl-tRNA to form a relatively stable complex, which is retained on cellulose nitrate filters. This reaction proceeds at both 0 degrees C and 37 degrees C and is inhibited by GTP. The resulting product is stabilized by GTP and Mg(2+). 2. Only very low quantities of deacylated tRNA are bound by transferase I. 3. Methods are described for the preparative isolation of the transferase I-aminoacyl-tRNA complex from incubation mixtures by using ion-exchange procedures. 4. The transferase I-aminoacyl-tRNA complex becomes readily bound to ribosomes. The presence of Mg(2+) is essential for the binding. GTP stimulates this reaction but is not absolutely required. 5. It is concluded that the formation of the transferase I-aminoacyl-tRNA complex may be the primary reaction in the binding of aminoacyl-tRNA to mammalian ribosomes and that, unlike in bacterial systems, GTP is not absolutely required for this step.
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D002850:Chromatography, Gel; D005260:Female; D006160:Guanosine Triphosphate; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism; D008274:Magnesium; D008297:Male; D010759:Phosphorus Isotopes; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D051381:Rats; D012270:Ribosomes / Q000378:metabolism*; D014166:Transferases
chemical_list: D000596:Amino Acids; D010759:Phosphorus Isotopes; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D014166:Transferases; D008274:Magnesium