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

Rudrabhatla, Parvathi and Rajasekharan, Ram (2002) Developmentally regulated dual-specificity kinase from peanut that is induced by abiotic stresses. In: Plant Physiology, 130 (1). pp. 380-390.


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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.

Item Type: Journal Article
Publication: Plant Physiology
Publisher: American Society of Plant Biologists
Additional Information: Copyright for this article belongs to American Society of Plant Biologists.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 09 Dec 2004
Last Modified: 19 Sep 2010 04:16
URI: http://eprints.iisc.ac.in/id/eprint/2001

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