Comparative phosphoproteome analysis of S. rimosus oxytetracycline producers strains
Principal investigator
The aim of this project is to determine the role of protein phosphorylation in antibiotic production from industrially important bacterium. Over the past decade phosphoproteomic studies of distantly related bacterial species have demonstrated protein phosphorylation on serine, threonine and tyrosine (Ser/Thr/Tyr) as widely employed posttranslational modification (PTM) of proteins which participate in various cellular processes, from basic metabolism to signaling and development. Recent advances in mass spectrometry-based proteomics has had a significant impact on rapid development of this field. Although this type of PTM is extensively used in bacteria and that there is a fast growing list of Ser/Thr/Tyr phosphorylated proteins, the extent and biological function of this PTM, in most cases, is not well defined. Therefore, this project will investigate the comparative phosphoproteome of Streptomyces rimosus strains that vary in the amounts of the antibiotic oxytetracycline (OTC) produced, in order to uncover the impact of this PTM on the antibiotic biosynthesis.