Furumoto T, Ogawa N, Hata S, Izui K
Laboratory of Applied Botany, Faculty of Agriculture, Kyoto University, Sakyo-ku, Japan.
FEBS Lett. 1996 Nov 4;396(2-3):147-51. doi: 10.1016/0014-5793(96)01090-3.
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.
在植物中,钙依赖蛋白激酶(CDPKs)构成了一个大家族,其特征是具有一个C端类钙调蛋白(CaM)结构域。最近,发现了一个编码非典型CDPK的新胡萝卜cDNA克隆,该克隆在类CaM结构域中具有明显退化的序列,并将其命名为CDPK相关蛋白激酶(CRK)[Lindzen, E.和Choi, J.H.(1995)植物分子生物学28, 785 - 797]。我们从玉米中获得了两个编码CRKs的不同cDNA克隆。为了对CRK进行首次酶学特性分析,将一个玉米cDNA克隆在大肠杆菌中表达。重组蛋白能有效地磷酸化酪蛋白,这是一种传统的蛋白质底物。值得注意的是,在这个体外磷酸化测定中,激酶活性不需要钙作为激活剂。因此,CRKs被认为是具有退化CaM结构域的新型钙非依赖性蛋白激酶,其功能仍有待阐明。