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

Jing Li | Zendy; Sarah M. Assmann | Zendy

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

Author(s) -

Jing Li,

Sarah M. Assmann

Publication year - 1996

Publication title -

the plant cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.324

H-Index - 341

eISSN - 1532-298X

pISSN - 1040-4651

DOI - 10.1105/tpc.8.12.2359

Subject(s) - guard cell , autophosphorylation , abscisic acid , biology , microbiology and biotechnology , phosphorylation , signal transduction , protein kinase a , biochemistry , threonine , protein phosphorylation , serine , gene

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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