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Nucleic Acids Research, 1978, Vol. 5, No. 3 861-877
© 1978

Articles

Properties of tRNAPhe from yeast carrying a spin label on the 3'-terminal. Interaction with yeast phenylalanyl-tRNA synthetase and elongation factor Tu from Escherichia coli

Mathias Sprinzl, Gunhild E. Siboska and Jens A. Pedersen

Max-Planck-Institut für Experimentelle Medizin, Abteilung chemie D-3400 Göttingen, GFR Department of chemistry, Aarhus University DK-8000 Aarhus C, Denmark

Received January 3, 1978. The 2-thioketo function of tRNA Phe-C-S2C-A in which the penultimate cytidine residue is replaced by 2-thiocytidine can serve as site of specific attachment of spin label. By alkylatio tPNAPhe-C-s2C-A with iodoacetamide or its spin label derivatives tRNAPhe-C-(acm) s2C-A or tRNAPhe C-(SL)s2C-A are formed. The enzymatic phenylalanylation of these tRNAsPhe revealed that the 2-position of the penultimate cytidine can be modified without impairing this enzymatic reaction but there exists a sterical limitation for the substituent on this position beyond which the tRNAphe:phenylalanyl-tRNA synthetase recogniition is not possible. Both Phe-tRNAPhe-C- (acm)s2C-A as well as Phe-tRNAPhe-C-(SL)s2C-A from ternary complexes with EF-Tu·GTP. The part of the 3'-terminus of tRNAPhe where the additional substituents are attached is therefore not involved in the interaction with this elongation factor. This could be also demonstrated by ESR of measurements of spin labelled tRNAsPhe. The correlation times, {tau} , for tRNAPhe-C-(SL)s2C-A, phe-tRNAPhe-C-(SL)s2C-A and Phe-tRNAPhe-C-(SL)s2C-Ac·EF-Tu:GTP are essentially identical indicating that the structure of the 3'-end of tRNAPhe is not influenced significantly by aminoacylation or ternary complex formation.


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