Thiostrepton, an Inhibitor of 50S Ribosome Subunit Function
AUTOR(ES)
Weisblum, B.
RESUMO
Thiostrepton inhibits 14C-leucine incorporation by intact cells of Bacillus megaterium as well as 14C-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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=250429Documentos Relacionados
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