Plant Physiology 98:708-715 (1992)
© 1992 American Society of Plant Biologists
Metabolism and Enzymology
-Furfuryl- -Glucoside: An Endogenous Activator of Higher Plant UDP-Glucose:(1-3)- -Glucan Synthase 1
Biological Activity, Distribution, and in Vitro Synthesis
Patricia Ohana,
Deborah P. Delmer,
Gail Volman,
John C. Steffens,
David E. Matthews and
Moshe Benziman
Department of Biological Chemistry, Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel,
Department of Botany, Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel,
Department of Plant Breeding and Biometry, New York State College of Agriculture and Life Science, Cornell University, 252 Emerson Hall, Ithaca, New York
In a recent paper (P Ohana, DP Delmer, JC Steffens, DE Matthews, R Mayer, M Benziman [1991] J Biol Chem 266: 13472-13475), we described the purification and structural characterization of -furfuryl- -glucoside (FG), an endogenous activator of plant UDP-glucose:(1 3)- -glucan (callose) synthase. In the present report, we provide evidence that FG specifically stimulates callose synthase. The effects of FG on the kinetic properties of callose synthase were studied, and we ascertained that FG, or at least a very similar compound, is present in other plant systems. Chemically synthesized -furfuryl- -glucoside also stimulates callose synthase, exhibiting a slightly higher Ka of 80 micromolar, compared with 50 micromolar for FG. In addition, we have identified and partially characterized an enzyme that catalyzes the synthesis of FG using -furfuryl alcohol and UDP-glucose as substrates. A model for the regulation of callose synthesis in vivo, involving changes in intracellular compartmentation of FG and Ca2+, is proposed.
1 P.O. and M.B. were supported by Weyerhaeuser Company, D.P.D. by a contract from the U.S. Department of Energy, and J.C.S. and D.E.M. were supported by Hatch project 149417.
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