Thiostrepton, an Inhibitor of 50 S Ribosome Subunit Function

Author:

Weisblum B.1,Demohn V.1

Affiliation:

1. Department of Pharmacology, University of Wisconsin Medical School, Madison, Wisconsin 53706

Abstract

Thiostrepton inhibits 14 C-leucine incorporation by intact cells of Bacillus megaterium as well as 14 C-phenylalanine incorporation by a poly U-directed extract of Escherichia coli . Extracts of E. coli which are pretreated by incubation with thiostrepton cannot be reactivated by dialysis to more than 5% of their former activity. The 50 S ribosome subunit appears to be the site of thiostrepton action, since protein-synthesizing activity can be restored to dialyzed pretreated extracts by supplementation with 50 S ribosome subunits but not with 30 S ribosome subunits. This technique also provides a simple sensitive method for detection of the biological activity of very small amounts of 50 S ribosome subunits.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference10 articles.

1. The structure of thiostrepton;Anderson B.;Nature (London),1970

2. Thiostrepton. Degradation products and structural features;Bodanszky M.;J. Amer. Chem. Soc.,1964

3. Subunit localization studies of antibiotic inhibitors of protein synthesis;Chang F. N.;Biochim. Biophys. Acta,1969

4. Lincomycin, an inhibitor of aminoacyl sRNA binding to ribosomes;Chang F. N.;Proc. Nat. Acad. Sci. U.S.A.,1965

5. The specificity of lincomycin binding to ribosomes;Chang F. N.;Biochemistry,1967

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