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Abstract
A soluble Ca 2+- and Ca 2+—calmodulin-activated protein kinase was partially purified from wheat germ. The phosphorylation of histones and casein catalyzed by this enzyme is largely Ca 2+-dependent. After repeated gel filtration of the protein kinase in the presence of 1 mM EGTA, the phosphorylation of casein and histones by the enzyme is activated 3-fold and up to 16-fold, respectively, by added calmodulin (12.5 μM). Such activation of the protein kinase by calmodulin is Ca 2+-dependent. The protein kinase binds to calmodulin—Sepharose 4B in a Ca 2+-dependent fashion. This type of Ca 2+-activated protein kinase may be involved in stimulus—response coupling in plants.
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