Open AccessMultiple phosphorylation of membrane‐associated calcium‐dependent protein serine/threonine kinase in Streptomyces fradiae
Author(s) -
Elizarov Sergey M.,
Danilenko Valery N.
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10793.x
Subject(s) - autophosphorylation , streptomyces fradiae , biochemistry , phosphorylation , protein phosphorylation , threonine , serine , biology , kinase , membrane protein , protein kinase a , chemistry , microbiology and biotechnology , membrane , streptomyces , actinomycetales , genetics , bacteria
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.