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 50S ribosome subunit appears to be the site of thiostrepton action, since protein-synthesizing activity can be restored to dialyzed pretreated extracts by supplementation with 50S ribosome subunits but not with 30S ribosome subunits. This technique also provides a simple sensitive method for detection of the biological activity of very small amounts of 50S ribosome subunits.
MeSH Terms
Anti-Bacterial Agents/pharmacology
Bacillus megaterium/drug effects,metabolism
Bacterial Proteins/biosynthesis
Carbon Isotopes
Depression, Chemical
Escherichia coli/drug effects,metabolism
Leucine/metabolism
Peptides/pharmacology
Phenylalanine/metabolism
Ribosomes/drug effects,physiology
Thymidine/metabolism
Uracil/metabolism
Chemicals
Anti-Bacterial Agents
Bacterial Proteins
Carbon Isotopes
Peptides
Phenylalanine
Uracil
Leucine
Thymidine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Weisblum B
Demohn V
References (8)
8 references, click to expand
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