Calmodulin-Like Activity Associated with Chromatin from Pea Buds

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NAD kinasc and cyclic AMP phosphodiesterase were activated by a factor prepared from pea chromatin. About 62% of the original amount of the factor in the purified chromatin was recovered in the reassociated chromatin. The NAD kinase- and cyclic AMP phosphodiesterase-activating factor was released from the chromatin by heat treatment with ethylene glycol-bis(β-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) then adsorbed on an affinity gel of phenothiazine-agarose derivatives in the presence of excess Ca^<2+> over EGTA, after which it was eluted by a flush of EGTA. Activation of NAD kinase and cyclic AMP phosphodiesterase by this factor depended on the presence of Ca^<2+>. The NAD kinase-activating factor and chromatin were coeluted when soluble chromatin was applied to a Bio-Gel A50 column. When chromatin was chromatographed on the same column after digestion by DNase I, the factor was eluted in association with the digested products of the chromatin. The activation properties of this factor indicate that a calmodulin-like activity exists in association with pea chromatin. The activation curves of cyclic AMP phosphodiesterase with the pea bud factor and with bovine brain calmodulin were compared. The amount of the factor in the chromatin fraction that corresponded to authentic calmodulin was calculated as 5.7 /μg per mg DNA.
日本植物生理学会の論文