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Nucleic Acids Research, 1990, Vol. 18, No. 23 6889-6893
© 1990

Articles

Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts

Marcus E. Peter, Christian O.A. Reiser, Norbert K. Schirmer, Thomas Kiefhaber, Günther Ott, Norbert W. Grillenbeck and Mathias Sprinzl*

Laboratorium für Biochemie, Universität Bayreuth Postfach 10 12 51, D-8580 Bayreuth, FRG

* To whom correspondence should be addressed

Received September 7, 1990. Revised October 23, 1990. Accepted October 23, 1990.

The middle and C-terminal domain (domain II/III) of elongation factor Tu from Thermus thermophilus lacking the GTP/GDP binding domain have been prepared by treating nucleotide-free protein with Staphylococcus aureus V8 protease. The isolated domain II/III of EF-Tu has a compact structure and high resistance against tryptic treatment and thermal denaturation. As demonstrated by circular dichroism spectroscopy, the isolated domain II/III does not contain any {alpha}-hellcal structure. Nucleotide exchange factor, EF-Ts, was found to Interact with domain II/III, whereas the binding of amlnoacyl-tRNA, GDP and GTP to this EF-Tu fragment could not be detected.


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