Evidence for phosphoprotein phosphatase in Streptomyces granaticolor.

The existence of phosphoprotein phosphatase (PPP) in aerial mycelium of S. granaticolor was demonstrated. Using inhibitors of serine and/or threonine PPP and specifically labeled substrate it was found that the PPP is of the serine and/or threonine type.

Pattern of phosphoproteins during cell differentiation in Streptomyces collinus.

Transition from vegetative cells to aerial mycelium and spores of Streptomyces collinus is accompanied by changes in the pattern of proteins phosphorylated. Preparation from spores exhibits lower phosphorylation activity than those of vegetative cells and aerial mycelium. Phosphorylation of proteins from aerial mycelium was markedly stimulated by the presence of Mn2+.

Improved method for rapid purification of protein kinase from streptomycetes.

Protein kinase from Streptomyces lincolnensis was purified nearly to homogeneity using a high performance liquid chromatography (HPLC) and a Pharmacia FPLC system. The procedure used employed column chromatography on DE-53, followed by FPLC affinity chromatography with serine- or threonine-Sepharose (prepared as described in this paper) and gel filtration using a Superose 12 or TSK G3000SW column. Starting with 3.

Effect of protein phosphorylation on the activity of RNA polymerase in streptomycetes.

RNA polymerase was isolated from Streptomyces granaticolor and protein kinase was partially purified from Streptomyces albus. When RNA polymerase was treated with protein kinase in vitro the activity of RNA polymerase was markedly enhanced. Furthermore, a protein of M = 65 kDa was isolated which, after being phosphorylated, stimulated RNA polymerase activity in vitro.

Protein phosphorylation in Streptomyces albus.

The phosphorylated proteins of Streptomyces albus, radioactively labeled with [32P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 protein species were found to be phosphorylated. With [32P]ATP as substrate cell free extracts phosphorylated endogenous proteins in vitro which were predominantly phosphorylated in vivo.