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Nucleic Acids Research, 1974, Vol. 1, No. 8 1079-1085
© 1974

Articles

Terminal oxidation-reduction of N-acetyl-phenylaianyl-tRNA blocks initiation complex formation with Escherichia coli 30S ribosomal subunits

James Ofengand and Zamirul Hussain*

Roche Institute of Molecular Biology Nutley, New Jersey 07110, USA *Primate Center, University of California Davis, California 95616, USA

Received July 16, 1974. Terminally oxidized-reduced tRNAPhe 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-tRNAox-red to form an initiation complex with Escherichia coli 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.


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