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THE PLANT CELL, Vol 9, Issue 5 809-824, Copyright © 1997 by American Society of Plant Biologists
Salicylic Acid Activates a 48-kD MAP Kinase in Tobacco
S. Zhang and D. F. Klessig
Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, P.O. Box 759, Piscataway, New Jersey 08855-0759
The involvement of phosphorylation/dephosphorylation in the salicylic acid
(SA) signal transduction pathway leading to pathogenesis-related gene
induction has previously been demonstrated using kinase and phosphatase
inhibitors. Here, we show that in tobacco suspension cells, SA induced a
rapid and transient activation of a 48-kD kinase that uses myelin basic
protein as a substrate. This kinase is called the p48 SIP kinase (for
SA-induced protein kinase). Biologically active analogs of SA, which induce
pathogenesis-related genes and enhanced resistance, also activated this
kinase, whereas inactive analogs did not. Phosphorylation of a tyrosine
residue(s) in the SIP kinase was associated with its activation. The SIP
kinase was purified to homogeneity from SA-treated tobacco suspension
culture cells. The purified SIP kinase is strongly phosphorylated on a
tyrosine residue(s), and treatment with either protein tyrosine or
serine/threonine phosphatases abolished its activity. Using primers
corresponding to the sequences of internal tryptic peptides, we cloned the
SIP kinase gene. Analysis of the SIP kinase sequence indicates that it
belongs to the MAP kinase family and that it is distinct from the other
plant MAP kinases previously implicated in stress responses, suggesting
that different members of the MAP kinase family are activated by different
stresses.
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