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An abscisic acid-activated and calcium-independent protein kinase from guard cells of fava bean
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An abscisic acid-activated and calcium-independent protein kinase from guard cells of fava bean
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Journal Article
An abscisic acid-activated and calcium-independent protein kinase from guard cells of fava bean
1996
Overview
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 (approx 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
