The putative anti-anti-sigma factor BldG is post-translationally modified by phosphorylation in Streptomyces coelicolor.
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.
Bignell
Dawn R D
DR
Department of Biological Sciences, CW405 Biological Sciences Building, University of Alberta, Edmonton, AB, Canada T6G 2E9.
Lau
Leon H
LH
Colvin
Kimberley R
KR
Leskiw
Brenda K
BK
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004269:DNA, Bacterial / Q000235:genetics; D058619:Maltose-Binding Proteins; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012694:Serine / Q000737:chemistry; D012808:Sigma Factor / Q000037:antagonists & inhibitors; D013302:Streptomyces / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004269:DNA, Bacterial; D058619:Maltose-Binding Proteins; D011993:Recombinant Fusion Proteins; D012808:Sigma Factor; D012694:Serine