Developmentally regulated dual-specificity kinase from peanut that is induced by abiotic stresses.

Tyrosine (Tyr) phosphorylation represents an important biochemical mechanism to regulate many cellular processes. No Tyr kinase has been cloned so far in plants. Dual-specificity kinases are reported in plants and the function of these kinases remains unknown. A 1.7-kb cDNA that encodes serine/threonine/Tyr (STY) kinase was isolated by screening peanut (Arachis hypogaea) expression library using the anti-phospho-Tyr antibody. The histidine-tagged recombinant kinase histidine-6-STY predominantly autophosphorylated on Tyr and phosphorylated the histone primarily on threonine. Genomic DNA gel-blot analysis revealed that STY kinase is a member of a small multigene family. The transcript of STY kinase is accumulated in the mid-maturation stage of seed development, suggesting a role in the signaling of storage of seed reserves. The STY kinase mRNA expression, as well as kinase activity, markedly increased in response to cold and salt treatments; however, no change in the protein level was observed, suggesting a posttranslational activation mechanism. The activation of the STY kinase is detected after 12 to 48 h of cold and salt treatments, which indicates that the kinase may not participate in the initial response to abiotic stresses, but may play a possible role in the adaptive process to adverse conditions. The transcript levels and kinase activity were unaltered with abscisic acid treatment, suggesting an abscisic acid-independent cold and salt signaling pathway. Here, we report the first identification of a non-MAP kinase cascade dual-specificity kinase involved in abiotic stress and seed development.