Protein phosphorylation in Streptomyces albus

Abstract

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. From cell extract which exhibited active phosphorylated in vitro, a protein kinase has been partially purified. The kinase activity was identified in fractions corresponding to a 90 kDa protein.

Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2)

“…Concomitant with morphological differentiation, these organisms undergo a biochemical differentiation during which they produce economically important secondary metabolites. Several studies have been carried out indicating that protein phosphorylation takes place in Streptomyces coelicolor and other streptomycetes (14,33,42,47), and a protein kinase that phosphorylates serine and threonine residues in vitro was discovered recently (33). Using monoclonal anti-phosphotyrosine (PY) antibodies 4G10 and IG2, Waters et al (47) recently showed evidence for protein tyrosine phosphorylation in Streptomyces hygroscopicus, Streptomyces griseus, Streptomyces lividans, and S. coelicolor.…”