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• W1577886434 startingPage "4089" @default.
• W1577886434 abstract "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." @default.
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• W1577886434 date "1998-08-15" @default.
• W1577886434 modified "2023-09-25" @default.
• W1577886434 title "Binding Interaction between Tet(M) and the Ribosome: Requirements for Binding" @default.
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• W1577886434 doi "https://doi.org/10.1128/jb.180.16.4089-4092.1998" @default.
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