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THE PLANT CELL, Vol 5, Issue 8 931-940, Copyright © 1993 by American Society of Plant Biologists
Identification and Characterization of High-Affinity Binding Sites for Inositol Trisphosphate in Red Beet
J. M. Brosnan and D. Sanders
Biology Department, University of York, York YO1 5DD, United Kingdom
Inositol 1,4,5-trisphosphate (InsP3) is thought to play a primary role in
intracellular Ca2+ mobilization during signal transduction in plant cells.
Although InsP3-elicited Ca2+ release across the vacuolar membrane has been
demonstrated in a variety of species, little is known of the properties of
the putative InsP3 receptor. Using a 3H-InsP3 ligand-displacement assay
with detergent-solubilized microsomes from the storage root of red beet, we
determined that InsP3 binds specifically to a single class of high-affinity
binding sites (dissociation constant [Kd] = 121 [plus or minus] 10 nM) with
an estimated receptor density of 0.84 pmol/mg. Binding of InsP3 is
selective, because other inositol phosphates exhibited only supramicromolar
affinities for the binding site. Low molecular weight heparin was a potent
competitive inhibitor of InsP3 binding (Kd = 301 [plus or minus] 72 nM).
High concentrations of ATP also displaced 3H-InsP3 (Kd = 0.66 mM).
Preincubation of microsomes with sulfhydryl reagents reduced InsP3-specific
binding in an InsP3-protectable manner. Density gradient centrifugation of
microsomes led to copurification of InsP3-specific binding with a fraction
enriched in vacuolar membrane. Despite a probable difference in cellular
location, the putative InsP3 receptor of red beet has characteristics that
are very similar to those of animal InsP3 receptors. These studies provide
direct evidence of InsP3-specific binding in plant tissue and strengthen
the argument that InsP3-induced Ca2+ release is a component in plant cell
signal transduction.
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