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Journal of Bacteriology, August 1998, p. 4089-4092, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Binding Interaction between Tet(M) and the Ribosome: Requirements for Binding

Kathi A. Dantley, H. Kathleen Dannelly,dagger and Vickers Burdett*

Department of Microbiology, Duke University Medical Center, Durham, North Carolina 27710

Received 17 February 1998/Accepted 11 June 1998

Tet(M) protein interacts with the protein biosynthesis machinery to render this process resistant to tetracycline by a mechanism which involves release of the antibiotic from the ribosome in a reaction dependent on GTP hydrolysis. To clarify this resistance mechanism further, the interaction of Tet(M) with the ribosome has been examined by using a gel filtration assay with radioactively labelled Tet(M) protein. The presence of GTP and 5'-guanylyl imido diphosphate, but not GDP, promoted Tet(M)-ribosome complex formation. Furthermore, thiostrepton, which inhibits the activities of elongation factor G (EF-G) and EF-Tu by binding to the ribosome, blocks stable Tet(M)-ribosome complex formation. Direct competition experiments show that Tet(M) and EF-G bind to overlapping sites on the ribosome.

* Corresponding author. Mailing address: Department of Microbiology, Duke University Medical Center, Durham, NC 27710. Phone: (919) 684-2944. Fax: (919) 681-8911. E-mail: burdett{at}abacus.mc.duke.edu.

dagger Present address: Department of Biological Sciences, Indiana State University, Terre Haute, IN 47809.

Journal of Bacteriology, August 1998, p. 4089-4092, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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