Related Experiment Video
Updated: Sep 20, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
The putative anti-anti-sigma factor BldG is post-translationally modified by phosphorylation in Streptomyces
Dawn R D Bignell1, Leon H Lau, Kimberley R Colvin
1Department of Biological Sciences, CW405 Biological Sciences Building, University of Alberta, Edmonton, AB, Canada T6G 2E9.
Abstract:
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.
Related Concept Videos
Bacterial RNA Polymerase
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
Coordination of Gene Expression Processes in Bacteria
Bacterial Protein Maturation
Stringent Response in E. coli
Other Stress Responses in Bacteria
Regulation of Bacterial Virulence

