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

Vincent Ling, Wayne A. Snedden, Barry J. Shelp and Sarah M. Assmann
The Plant Cell
Vol. 6, No. 8 (Aug., 1994), pp. 1135-1143
DOI: 10.2307/3869891
Stable URL: http://www.jstor.org/stable/3869891
Page Count: 9
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Analysis of a Soluble Calmodulin Binding Protein from Fava Bean Roots: Identification of Glutamate Decarboxylase as a Calmodulin-Activated Enzyme
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Abstract

The identity of a soluble 62-kD Ca2+-dependent calmodulin binding protein (CaM-BP) from fava bean seedlings was determined. Using 125 I- 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 α-decarboxylation of glutamate to form the stress-related metabolite γ-aminobutyrate. Activity assays of partially purified, desalted, root GAD revealed a 50% stimulation by the addition of 100 μM Ca2+, a 100% stimulation by the addition of 100 μM 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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