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Plant Cell, Vol. 12, 165-178, January 2000, Copyright © 2000, American Society of Plant Physiologists

Osmotic Stress Induces Rapid Activation of a Salicylic Acid–Induced Protein Kinase and a Homolog of Protein Kinase ASK1 in Tobacco Cells

Monika Mikolajczyka, Olubunmi S. Awotundea, Grazyna Muszynskaa, Daniel F. Klessigb, and Grazyna Dobrowolskaa
a Institute of Biochemistry and Biophysics, Polish Academy of Sciences, ul. Pawinskiego 5a, 02-106 Warsaw, Poland
b Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, 190 Frelinghuysen Road, Piscataway, New Jersey 08854-8020

Correspondence to: Grazyna Dobrowolska, dobrowol{at}ibb.waw.pl (E-mail), 48-22-39-12-16-23 (fax)

In tobacco cells, osmotic stress induced the rapid activation of two protein kinases that phosphorylate myelin basic protein. Immunological studies demonstrated that the 48-kD kinase is the salicylic acid–induced protein kinase (SIPK), a member of the mitogen-activated protein kinase family. SIPK was activated 5 to 10 min after the cells were exposed to osmotic stresses, and its activity persisted for ~30 min. In contrast, the 42-kD kinase was activated within 1 min after osmotic stress, and its activity was maintained for ~2 hr. Moreover, in addition to myelin basic protein, the 42-kD kinase phosphorylated casein and two transcription factors, c-Jun and ATF-2. This latter enzyme was inactivated by a serine/threonine–specific phosphatase but, unlike SIPK, was not affected by a tyrosine-specific phosphatase. After the 42-kD kinase was purified to apparent homogeneity, tryptic peptide analysis indicated that it is a homolog of Arabidopsis serine/threonine kinase1 (ASK1).




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