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. 1980 Oct 24;8(20):4737–4744. doi: 10.1093/nar/8.20.4737

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

M Sprinzl, E Graeser
PMCID: PMC324383  PMID: 7003543

Abstract

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 rRNA 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 aminoacylation is not affected.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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