Abstract
In plants, calcium-dependent protein kinases (CDPKs) make up a large family that is characterized by a C-terminal calmodulin(CaM)-like domain. Recently, a novel carrot cDNA clone encoding an atypical CDPK, which has a significantly degenerate sequence in the CaM-like domain, was found and named CDPK-related protein kinase (CRK) [Lindzen, E. and Choi, J.H. (1995) Plant Mol. Biol. 28, 785–797]. We obtained two different cDNA clones from maize which encode CRKs. For the first enzymatic characterization of CRK, a maize cDNA clone was expressed in E. coli. The recombinant protein efficiently phosphorylated casein, a conventional protein substrate. Notably, in this in vitro phosphorylation assay, the kinase activity did not require calcium as an activator. Thus, CRKs were suggested to be novel calcium-independent protein kinases having a degenerate CaM domain, the function of which remains to be elucidated.
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