title: 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.
abstract: 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.
mesh_terms: 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
chemical_list: 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