PROTEIN-PHOSPHORYLATION IN SUBMERGED SPORES AND VEGETATIVE MYCELIUM OF STREPTOMYCES GRANATICOLOR

Transfer of phosphate from gamma-[P-32]ATP to endogenous proteins cata lysed by cell-free extracts was used as a tool for studies of protein phosphorylation via protein kinases in streptomycetes. Thus, phosphopr oteins were detected in submerged spores and vegetative mycelium of St reptomyces granaticolor which were identified as O-phosphomonoesters r ather than N-phosphates or acyl phosphates. The extent and pattern of phosphorylation was dependent on the growth stage of the culture and w as greatly enhanced by Mn2+.