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

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1998 Aug 8

PMID 9696754

Citations 12

Authors

K A Dantley

H K Dannelly

V Burdett

Affiliations

Soon will be listed here.

Abstract

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.

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