Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans.
AUTOR(ES)
Holmes, D J
RESUMO
Although the antibiotic thiostrepton is best known as an inhibitor of protein synthesis, it also, at extremely low concentrations (< 10(-9) M), induces the expression of a regulon of unknown function in certain Streptomyces species. Here, we report the purification of a Streptomyces lividans thiostrepton-induced transcriptional activator protein, TipAL, whose N-terminus is similar to a family of eubacterial regulatory proteins represented by MerR. TipAL was first purified from induced cultures of S.lividans as a factor which bound to and activated transcription from its own promoter. The tipAL gene was overexpressed in Escherichia coli and TipAL protein purified in a single step using a thiostrepton affinity column. Thiostrepton enhanced binding of TipAL to the promoter and catalysed specific transcription in vitro. TipAS, a second gene product of the same open reading frame consisting of the C-terminal domain of TipAL, is apparently translated using its own in-frame initiation site. Since it is produced in large molar excess relative to TipAL after induction and also binds thiostrepton, it may competitively modulate transcriptional activation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=413584Documentos Relacionados
- Thiostrepton-induced gene expression in Streptomyces lividans.
- Heterologous activation of the actinorhodin biosynthetic pathway in Streptomyces lividans.
- Cloning, sequencing, and expression of a Thermomonospora fusca protease gene in Streptomyces lividans.
- Glycosylation of macrolide antibiotics in extracts of Streptomyces lividans.
- Cloning, expression, and characterization of the Micromonospora viridifaciens neuraminidase gene in Streptomyces lividans.