Role of the 5'-terminal phosphate of tRNA for its function during protein biosynthesis elongation cycle.
The 5'-terminal phosphate of tRNAPhe from yeast was removed using tRNAPhe lacking its 3'-terminal adenosine. After regeneration of the C-C-A terminus this tRNA was investigated in following reactions: aminoacylation, spontaneous hydrolysis of the amino acid from aminoacyl-tRNA, aminoacyl-tRNA.EF-Tu.GTP ternary complex formation and poly(U)-dependent synthesis of poly(Phe). The absence of the 5'-terminal phosphate of Phe-tRNAPhe does not influence the rate of hydrolysis of the amino acid or the ability of this rRNA to participate in complex formation with EF-Tu.GTP. The translation of the polyuridylic acid is slightly inhibited whereas the rate and extent of the enzymatic aminoacylation is not affected.
D001426:Bacterial Proteins; D004926:Escherichia coli / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D009943:Organophosphorus Compounds; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu; D010649:Phenylalanine; D012343:RNA, Transfer / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D001426:Bacterial Proteins; D009943:Organophosphorus Compounds; D012346:RNA, Transfer, Amino Acyl; D010649:Phenylalanine; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D010444:Peptide Elongation Factor Tu