The putative anti-anti sigma factor BldG is post-translationally modified by phosphorylation in Streptomyces coelicolor

Author
Harcombe, Kimberley
Bignell, D. R. D.
Lau, L. H.
Leskiw, B. K.
Faculty Advisor
Date
2003
Keywords
bldG gene , antibiotics
Abstract (summary)
The Streptomyces coelicolor bldG gene encodes a protein showing similarity to the SpoIIAA and RsbV anti-anti-sigma factors of Bacillus subtilis. Purified maltose binding protein-BldG could be phosphorylated in vitro by wild-type S. coelicolor crude extract, and both the phosphorylated and unphosphorylated forms of BldG could be detected in vivo using isoelectric focusing. ATP was shown to serve as the phosphoryl group donor, and phosphorylation of BldG was abolished when the putative phosphorylation site was changed from a serine to an alanine residue. A bldG mutant strain expressing the non-phosphorylatable BldG protein was unable to undergo morphological differentiation or produce antibiotics even after prolonged incubation, suggesting that phosphorylation of BldG is necessary for proper development in S. coelicolor.
Publication Information
Bignell, D. R. D., Lau, L. H., Colvin, K. R., & Leskiw, B. K. (2003). The putative anti-anti sigma factor BldG is post-translationally modified by phosphorylation in Streptomyces coelicolor. FEMS Microbiology Letters, 225(1), 93-99.
DOI
Notes
Item Type
Article
Language
English
Rights
All Rights Reserved