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Nucleic Acids Research, 1988, Vol. 16, No. 21 10183-10197
© 1988

MOLECULAR BIOLOGY

The elongation factor EF-Tu from E.coli binds to the upstream activator region of the tRNA-tufB operon

E. Vijgenboom, L. Nilsson and L. Bosch

Department of Biochemistry, University of Leiden Wassenaarseweg 64, 2333 AL Leiden, The Netherlands

Received July 12, 1988. Accepted September 28, 1988.

The polypeptide chain elongation factor EF-Tu of Eschericbia coli is encoded by two genes, tufA and tufB, located in two different operons. Experiments in which either tufA or tufB was inactivated demonstrated that expression of the tRNA-tufB operon is dependent on a functioning tufA and thus on EF-Tu (1, to be published).

In order to study a possible role of EF-Tu as trans-activator of the tRNA-tufB operon, we have investigated in vitro binding of an EF-Tu. GDP preparation to various DNA fragments of the operon. We demonstrate that specific binding occurs to a cis-acting region delimited from position –134 to the promoter, previously shown to enhance tufB transcription (2).

Electrophoretic retardation assays reveal the formation of maximally three protein/DNA complexes, indicating that more than one protein molecule can bind to the DNA. The EF-Tu preparation used was obtained by affinity chromatography and appeared to be 95% pure. It lost its DNA binding activity upon further purification. That EF-Tu is nonetheless involved in the DNA binding is suggested by the observation that none of the three complexes is formed in the preaence of kirromycin, an antibiotic that binds EF-Tu with high specificity. If so, EF-Tu.GDP most likely binds to the activator region of the tRNA-tufB operon in combination with another non-identified protein or component.


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