Open AccessIdentification of Ca 2+ /calmodulin‐dependent protein kinase and endogenous substrate of Fusarium oxysporum
Author(s) -
Hoshino Tamotsu,
Mizutani Akihiro,
Hidaka Hiroyoshi,
Yamane Tsuneo
Publication year - 1992
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.1574-6968.1992.tb05283.x
Subject(s) - protein kinase a , calmodulin , biochemistry , biology , phosphorylation , fusarium oxysporum , camk , peptide sequence , microbiology and biotechnology , protein phosphorylation , endogeny , kinase , binding protein , enzyme , botany , gene , autophosphorylation
Ca 2+ /calmodulin‐dependent phosphorylation and cross‐reactivity between anti‐rat brain Ca 2+ /calmodulin‐dependent protein kinase II (CaMK) antibody and partially purified CaMK from Fusarium oxysporum were detected in the component of high‐molecular mass (M r > 100 000). In vitro, Ca 2+ /CaM‐dependent phosphorylation of only a 16‐kDa protein was detected. The 16‐kDa protein was localized in the membrane fraction. Amino acid sequence of one of the peptides derived from partial hydrolysis of the 16‐kDa protein had a high homology (65.5%) with the bovine transducin β chain. It is assumed that the 16‐kDa protein is an endogenous substrate of F. oxysporum CaMK.