Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine.
A method is presented by which the site of primary attachment of the amino acids with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine of E. coli tRNAs can be determined. It is found that the aminoacyl-tRNA synthetases (EC 6.1.1.-) with specificity for Arg, Asn, Ile, Leu, Met, Phe, Thr, Trp, and Val attach the amino acid to the 2'-position; those with specificity for Gly, His, Lys, and Ser attach the amino acid to the 3'-position; and that Tyr and Cys can be enzymatically attached to both the 2'- and 3'-positions. Together with previous experiments on yeast aminoacyl-tRNA synthetases, it is now shown that the specificity for one particular hydroxyl group is preserved during the evolution from prokaryotic to eukaryotic systems.
D000241:Adenosine / Q000032:analysis; D000596:Amino Acids; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology*; D008099:Liver / Q000201:enzymology; D012343:RNA, Transfer / Q000032:analysis*; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013045:Species Specificity; D046249:Transfer RNA Aminoacylation
D000596:Amino Acids; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases; D000241:Adenosine