Identification of Ca2+/calmodulin-dependent protein kinase and endogenous substrate of Fusarium oxysporum.
Ca2+/calmodulin-dependent phosphorylation and cross-reactivity between anti-rat brain Ca2+/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) greater than 100,000). In vitro, Ca2+/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 beta chain. It is assumed that the 16-kDa protein is an endogenous substrate of F. oxysporum CaMK.
Hoshino
T
T
Department of Food Science and Technology, School of Agriculture, Nagoya University, Japan.
Mizutani
A
A
Hidaka
H
H
Yamane
T
T
D000595:Amino Acid Sequence; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D005656:Fungal Proteins; D005670:Fusarium / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry* / Q000302:isolation & purification / Q000502:physiology; D013379:Substrate Specificity
D005656:Fungal Proteins; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases