THE PLANT CELL, Vol 8, Issue 12 2359-2368, Copyright © 1996 by American Society of Plant Biologists

RESEARCH ARTICLES

An Abscisic Acid-Activated and Calcium-Independent Protein Kinase from Guard Cells of Fava Bean

J. Li and S. M. Assmann
Department of Biology and Plant Physiology Program, Pennsylvania State University, University Park, Pennsylvania 16802

Abscisic acid (ABA) regulation of stomatal aperture is known to involve both Ca2+-dependent and Ca2+-independent signal transduction pathways. Electrophysiological studies suggest that protein phosphorylation is involved in ABA action in guard cells. Using biochemical approaches, we identified an ABA-activated and Ca2+- independent protein kinase (AAPK) from guard cell protoplasts of fava bean. Autophosphorylation of AAPK was rapidly (~1 min) activated by ABA in a Ca2+- independent manner. ABA-activated autophosphorylation of AAPK occurred on serine but not on tyrosine residues and appeared to be guard cell specific. AAPK phosphorylated histone type III-S on serine and threonine residues, and its activity toward histone type III-S was markedly stimulated in ABA-treated guard cell protoplasts. Our results suggest that AAPK may play an important role in the Ca2+-independent ABA signaling pathways of guard cells.

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