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Nucleic Acids Research, 1980, Vol. 8, No. 20 4737-4744
© 1980

MOLECULAR BIOLOGY

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

Mathias Sprinzl* and Erika Graeser

Max-Planck-Institut für experimentelle Medizin Abteilung Chemie, Hermann-Rein-Str. 3, D-3400 Göttingen *Laboratorium für Biochemie der Universität Bayreuth D-8580 Bayreuth, GFR

Received August 27, 1980. The 5'-terminal phosphate of tRNAPhe from yeast was removed using tRNAPhe 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-tRNAPhe 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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