Plant Cell Journal of Pharmacology and Experimental Therapeutics
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THE PLANT CELL, Vol 6, Issue 8 1135-1143, Copyright © 1994 by American Society of Plant Biologists

RESEARCH ARTICLES

Analysis of a Soluble Calmodulin Binding Protein from Fava Bean Roots: Identification of Glutamate Decarboxylase as a Calmodulin-Activated Enzyme

V. Ling, W. A. Snedden, B. J. Shelp and S. M. Assmann
Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, Massachusetts 02138

The identity of a soluble 62-kD Ca2+-dependent calmodulin binding protein (CaM-BP) from fava bean seedlings was determined. Using 125I-CaM overlay assays, a class of soluble CaM-BPs was detected in extracts of tissues comprising the axis of 1.5-week-old seedlings, excluding the root tip and emergent leaves. The size of these CaM-BPs was not uniform within all parts of the plant; the apparent molecular masses were 62 kD in roots, 60 kD in stems, and 64 kD in nodules. The root 62-kD CaM-BP was purified, and internal microsequence analysis was performed on the protein. A tryptic peptide derived from the CaM-BP consisted of a 13-residue sequence corresponding to a highly conserved region of glutamate decarboxylase (GAD), an enzyme that catalyzes the [alpha]-decarboxylation of glutamate to form the stress-related metabolite [gamma]-aminobutyrate. Activity assays of partially purified, desalted, root GAD revealed a 50% stimulation by the addition of 100 [mu]M Ca2+, a 100% stimulation by the addition of 100 [mu]M Ca2+ plus 100 nM CaM, and no appreciable stimulation by CaM in the absence of added Ca2+. The demonstration that plant GAD is a Ca2+-CaM-stimulated enzyme provides a model in which stress-linked metabolism is modulated by a Ca2+-mediated signal transduction pathway.


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