Protein kinase activities in cell-free extracts of Streptomyces coelicolor A3(2).

Protein kinase activities were detected in cell-free extracts of the B385 derivative of Streptomyces coelicolor A3(2); at least 12 polypeptides, ranging in Mr from 6,000 to 98,000, were detectably phosphorylated, probably as O-monoesters, after incubation with gamma [32P]ATP. The culture stage of the mycelia used for production of the cell-free extracts determined the profile of phosphorylated polypeptides. Phosphoenol pyruvate acted as a potent modulator of the apparent degree of protein kinase activity. In addition Ca2+ ions, verapamil, chlorpromazine and anti-calmodulin antiserum had specific effects on the profile of phosphopolypeptides observed.