Characterization of the plant nicotinamide adenine dinucleotide kinase activator protein and its identification as calmodulin

Abstract

A protein activator of plant NAD kinase has been extracted from plant sources (peanuts and peas), purified to homogeneity, characterized, and identified as calmodulin. A comparison of the properties of calmodulin isolated from either plant or animal sources shows that they are strikingly similar proteins. The similarities include molecular weight, Stokes radii, amino acid composition, Ca2+-dependent enhancement of tyrosine fluorescence, Ca2+-dependent interaction with troponin I, equal abilities to activate cyclic nucleotide phosphodiesterase, Ca2+-dependent inhibition of calmodulin action by the phenothiazine drugs, and electrophoretic mobility. We discuss the possibility that plant cells may undergo Ca2+-dependent regulatory events that are mediated by calmodulin in a manner similar to those found in animals.