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• W1544146860 abstract "Abstract Two transfer factors, designated FIs and FIu, which are required for the guanosine triphosphate-dependent, messenger RNA-directed binding of aminoacyl transfer RNA to ribosomes, are also required for maximal interaction with GTP to form a complex that is retained by a nitrocellulose filter. This complex subsequently interacts with aminoacyl-tRNA to form a second complex that is not retained by a nitrocellulose filter and that can be recovered from the filtrate by gel filtration. This second complex is composed of aminoacyl-tRNA, GTP, and the heat-labile transfer factor, FIu. The GTP moiety of the complex does not exchange with GTP or other guanine nucleotides even at 37°; however, the aminoacyl-tRNA moiety of the complex dissociates and exchanges with other aminoacyl-tRNAs at 25° or 37° but does not rapidly exchange at 0°. At 0° preferential binding of the aminoacyl-tRNA moiety of the complex to ribosomes can be demonstrated in the presence of free aminoacyl-tRNA. These data provide evidence that the aminoacyl-tRNA-GTP-FIu complex is an intermediate in the GTP-dependent binding of aminoacyl-tRNA to ribosomes. The binding of the aminoacyl-tRNA moiety of the complex to ribosomes is inhibited by chlortetracycline but not by deacylated tRNA. In contrast, nonenzymatic binding of aminoacyl-tRNA to ribosomes is inhibited by deacylated tRNA but not by chlortetracycline. The binding of the aminoacyl-tRNA moiety of the complex to ribosomes occurs with the concomitant formation of Pi and a third complex composed of FIu and GDP. This FIu-GDP complex is retained by a nitrocellulose filter but does not appear to be bound to the ribosomal complex." @default.
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• W1544146860 date "1969-09-01" @default.
• W1544146860 modified "2023-09-30" @default.
• W1544146860 title "Formation and Properties of the Aminoacyl Transfer Ribonucleic Acid-Guanosine Triphosphate-Protein Complex" @default.
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• W1544146860 doi "https://doi.org/10.1016/s0021-9258(18)93662-8" @default.
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