Role of the 5′-terminal phosphate of tRNA for its function during protein biosynthesis elongation cycle

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Abstract
The 5′-terminal phosphate of tRNA Phe from yeast was removed using tRNA Phe lacking its 3′-terminal adenosine. After regeneration of the C-C-A terminus this tRNA was investigated in following reactions: aminoacylation, spontaneous hydrolysis of the amino acid from aminoacyl-tRNA, aminoacyl-tRNA·EF-Tu·GTP ternary complex formation and poly (U)-dependent synthesis of poly(Phe). The absence of the 5′-terminal phosphate of Phe-tRNA Phe does not influence the rate of hydrolysis of the amino acid or the ability of this tRNA to participate in complex formation with EF-Tu·GTP. The translation of the polyuridylic acid is slightly inhibited whereas the rate and extent of the enzymatic aminocylation is not affected.

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