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. 1971 Aug;68(8):1796–1800. doi: 10.1073/pnas.68.8.1796

Inhibition by Siomycin and Thiostrepton of Both Aminoacyl-tRNA and Factor G Binding to Ribosomes

Juan Modole Ll *, Bartolomé Cabrer *, Andrea Parmeggiani , David V Azquez *
PMCID: PMC389295  PMID: 4331558

Abstract

Siomycin, a peptide antibiotic that interacts with the 50S ribosomal subunit and inhibits binding of factor G, is shown also to inhibit binding of aminoacyl-tRNA; however, it does not impair binding of fMet-tRNA and completion of the initiation complex. Moreover, unlike other inhibitors of aminoacyl-tRNA binding (tetracycline, sparsomycin, and streptogramin A), siomycin completely abolishes the GTPase activity associated with the binding of aminoacyl-tRNA catalyzed by factor Tu. A single-site interaction of siomycin appears to be responsible for its effect on both the binding of the aminoacyl-tRNA-Tu-GTP complex and that of factor G.

Keywords: Millipore filter, Tu, tetracycline, streptogramin, puromycin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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