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Nucleic Acids Research, 1990, Vol. 18, No. 3 437-441
© 1990

MOLECULAR BIOLOGY

The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy

Günther Ott1, Jiri Jonák2, Ian Peter Abrahams3 and Mathias Sprinzl1,*

1Laboratorium für Biochemie der Universität Bayreuth Postfach 10 12 51, D-8580 Bayreuth, FRG, Czechoslovakia 2institute of Molecular Genetics, Czechoslovak Acad. Sci. Flemingovo nam.2 16637 Prague 6, Czechoslovakia 3Biochemisch Labortorium, Rijksuniversiteit Leiden Wassenaarseweg 64, NL-2333 Leiden AL, The Netherlands

* To whom correspondence should be addressed

Received November 21, 1989. Accepted December 28, 1989.

A fluorescence titration assay was used to detect the effects of various modifications of E.coli elongation factor Tu on the formation of the ternary complex with aminoacyl-tRNAs. The treatment of EF-Tu-GDP with TPCK, an analogue of the 3'terminus of aminoacyl-tRNA, was found to have no influence on the conversion of EF-Tu-GDP to ‘active’ EF-Tu-GTP, but does decrease the affinity of the activated protein for yeast aminoacyl-tRNA by more than three orders of magnitude. Modification of the elongation factor by limited cleavage with trypsin, leading to the excission of amino acid residues 45–58, has only a minor influence on ternary complex formation. The equilibrium dissociation constant of the ternary complex with this trypsin-treated EF-Tu GTP and E.coli Phe-tRNAPhe is only one order of magnitude higher than that of the ternary complex with native EF-Tu. Mutations in the amino acid residues 222 and 375 of EF-Tu also have little effect on ternary complex formation. Compared with TPCK-treated EF-Tu, the affinities of the two mutant species, designated EF-tuAR and EF-TuBo respectively, for [AEDANS-s2C]Tyr-tRNATyr are only slightly reduced and in the same range as trypsin-cleaved EF-Tu.


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