Interaction of aminoacyl-tRNA with bacterial elongation factor Tu: GTP complex: effects of the amino group of amino acid esterified to tRNA, the amino acid side chain, and tRNA structure.
The present investigation was undertaken to see to what extent the alpha-amino group of the amino acid, the side chain of the amino acid of aminoacyl-tRNA, and the tRNA structure are involved in determining the affinity of aminoacyl-tRNA for bacterial elongation factor Tu-GTP complex. Various aminoacyl-tRNAs, mis-aminoacylated tRNAs, and formylated aminoacyl-tRNAs were prepared, and the dissociation constants of the ternary complexes of aminoacyl-tRNA with ET-Tu: GTP were determined by the RNase-resistance assay. The results indicated that the free amino-acid group of the amino acids in aminoacyl-tRNA is strongly required for binding with EF-Tu : GTP. In this concentration, the biological significance of formylation for Met-tRNAMetf species is discussed.
D000596:Amino Acids / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000032:analysis; D004951:Esterification; D005575:Formyltetrahydrofolates; D006160:Guanosine Triphosphate / Q000378:metabolism*; D046911:Macromolecular Substances; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012358:RNA, Transfer, Met; D012260:Ribonucleases / Q000494:pharmacology; D013329:Structure-Activity Relationship
D000596:Amino Acids; D005575:Formyltetrahydrofolates; D046911:Macromolecular Substances; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; C024988:tRNA, formylmethionine-; D006160:Guanosine Triphosphate; D012260:Ribonucleases; D010444:Peptide Elongation Factor Tu