Terminal oxidation-reduction of N-acetyl-phenylalanyl-tRNA blocks initiation complex formation with Escherichia coli 30S ribosomal subunits.
Terminally oxidized-reduced tRNA(Phe) of yeast, exclusively acylated at the 2'-hydroxyl of the 3'-terminal ribose of the tRNA, is a useful model for investigating the stereospecificity of AA-tRNA in protein synthesis. In this work, the ability of N-acetyl-Phe-tRNA(ox-red) to form an initiation complex with Escherichiacoli 30S ribosomal subunits was investigated. Thirty per cent of added control N-acetyl-Phe-tRNA was bound in a reaction dependent on initiation factors, GTP, and poly U, but no binding of the oxidized-reduced analog could be detected. These results imply that initiation complex formation may be specific for the 3'-ester of initiator tRNA.
Ofengand
J
J
Hussain
Z
Z
D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism; D010084:Oxidation-Reduction; D010442:Peptide Chain Initiation, Translational; D012331:RNA, Fungal / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism*
D012331:RNA, Fungal; D012346:RNA, Transfer, Amino Acyl; C006383:tRNA, N-acetylphenylalanine-