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

dc.contributor.authorHarcombe, Kimberley
dc.contributor.authorBignell, D. R. D.
dc.contributor.authorLau, L. H.
dc.contributor.authorLeskiw, B. K.
dc.date.accessioned2022-05-31T00:00:40Z
dc.date.available2022-05-31T00:00:40Z
dc.date.issued2003
dc.description.abstractThe 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.
dc.description.urihttps://library.macewan.ca/cgi-bin/SFX/url.pl/9JU
dc.identifierhttps://doi.org/10.1016/S0378-1097(03)00504-4
dc.identifier.citationBignell, 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. https://doi.org/10.1016/S0378-1097(03)00504-4
dc.identifier.urihttps://hdl.handle.net/20.500.14078/1132
dc.languageEnglish
dc.language.isoen
dc.rightsAll Rights Reserved
dc.subjectbldG gene
dc.subjectantibiotics
dc.titleThe putative anti-anti sigma factor BldG is post-translationally modified by phosphorylation in Streptomyces coelicolor
dc.typeArticle
dspace.entity.type
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