Multiple phosphorylation of membrane-associated calcium-dependent protein serine/threonine kinase in Streptomyces fradiae.
In Streptomyces fradiae, calcium ions induce alterations in intensity and specificity of the secondary metabolism and stimulate aerial mycelium formation and sporulation. Using in vitro labeling, we demonstrate that in S. fradiae in the late exponential growth phosphorylation of 65-kDa membrane-associated protein is also influenced by Ca(2+) added exogenously. Calcium ions at physiological concentration stimulate intensive Ca(2+)-dependent phosphorylation of 65-kDa protein at multiple sites on serine, threonine, and tyrosine residues. Assay of protein kinases in situ demonstrated in the fraction of membrane-associated proteins the presence of two autophosphorylating protein serine/threonine kinases with molecular masses of 127 kDa and 65 kDa. Autophosphorylation of both proteins is also Ca(2+)-dependent.
Elizarov
S M
SM
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. inbio@glas.apc.org
Danilenko
V N
VN
D001345:Autoradiography; D002118:Calcium / Q000378:metabolism / Q000494:pharmacology*; D002474:Cell-Free System; D008970:Molecular Weight; D010766:Phosphorylation / Q000187:drug effects; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D019000:Phosphotyrosine / Q000378:metabolism; D011489:Protein Denaturation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology*
D010769:Phosphothreonine; D010768:Phosphoserine; D019000:Phosphotyrosine; D017346:Protein Serine-Threonine Kinases; D002118:Calcium