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Journal of Bacteriology, April 2001, p. 2700-2703, Vol. 183, No. 8
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.8.2700-2703.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Purification of the RelB and RelE Proteins of Escherichia coli: RelE Binds to RelB and to Ribosomes

Cheryl Galvani, Jefferson Terry, and Edward E. Ishiguro*

Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada V8W 3P6

Received 3 October 2000/Accepted 30 January 2000

The direct interaction of the Escherichia coli cytotoxin RelE with its specific antidote, RelB, was demonstrated in two ways: (i) copurification of the two proteins and (ii) a positive yeast two-hybrid assay involving the relB and relE genes. In addition, the purified RelE protein exhibited ribosome-binding activity in an in vitro assay, supporting previous observations suggesting that it is an inhibitor of translation.

* Corresponding author. Mailing address: Department of Biochemistry and Microbiology, University of Victoria, P.O. Box 3055, Victoria, B.C. V8W 3P6, Canada. Phone: (250) 721-7077. Fax: (250) 721-8855. E-mail: eishuv{at}uvvm.uvic.ca.

Journal of Bacteriology, April 2001, p. 2700-2703, Vol. 183, No. 8
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.8.2700-2703.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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