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Nucleic Acids Research, 1988, Vol. 16, No. 2 413-424
© 1988

Articles

Mechanism of autonomous control of the Escherichia coli F plasmid: purification and characterization of the repE gene product

Luke Masson* and Dan S. Ray

Department of Biology and Molecular Biology Institute, University of California Los Angeles, CA 90024, USA *Present address: Genetic Engineering Sention, Biotechnology Research Institute, National Research Council of Canada 6100 Royalmount Avenue, Mountreal, Quebec H4P 2R2, Canada

Received November 9, 1987. Accepted December 2, 1987.

E protein, the 29 Kd repE gene product, is essential for the replication of the Escherichia coli F plasmid. The repE gene has been cloned and expressed in an inducible ATG-fusion vector, and the protein product has been purified to homogeneity. The purified E protein is present as a dimer in solution and binds specifically to both the 19-bp direct repeats (incB) found within the mini-F origin of replication ori2 and the repE operator DNA. Examination of the ami no acid sequence of E protein revealed a consensus sequence for DNA binding.


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