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J Biol Chem, Vol. 274, Issue 9, 5738-5745, February 26, 1999

A Plant 126-kDa Phosphatidylinositol 4-Kinase with a Novel Repeat Structure
CLONING AND FUNCTIONAL EXPRESSION IN BACULOVIRUS-INFECTED INSECT CELLS

Hong-Wei Xue, Christophe Pical^¶, Charles Brearley^**, Stephan Elge, and Bernd Müller-Röber

From the  Max Planck Institute of Molecular Plant Physiology (MPI-MOPP), Karl-Liebknecht-Strae 25, Haus 20, D-14476 Golm/Potsdam, Germany, ^¶ University of Lund, Plant Biochemistry, P. O. Box 117, S.E. 22100 Lund, Sweden, and ^** Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom

Phosphatidylinositol metabolism plays a central role in signaling pathways in animals and is also believed to be of importance in signal transduction in higher plants. We report here the molecular cloning of a cDNA encoding a previously unidentified 126-kDa phosphatidylinositol (PI) 4-kinase (AtPI4K) from the higher plant Arabidopsis thaliana. The novel protein possesses the conserved domains present in animal and yeast PI 4-kinases, namely a lipid kinase unique domain and a catalytic domain. An additional domain, approximately 300 amino acids long, containing a high percentage (46%) of charged amino acids is specific to this plant enzyme. Recombinant AtPI4K expressed in baculovirus-infected insect (Spodoptera frugiperda) cells phosphorylated phosphatidylinositol exclusively at the D4 position of the inositol ring. Recombinant protein was maximally activated by 0.6% Triton X-100 but was inhibited by adenosine with an IC₅₀ of ~200 µM. Wortmannin at a concentration of 10 µM inhibited AtPI4K activity by ~90%. AtPI4K transcript levels were similar in all tissues analyzed. Light or treatment with hormones or salts did not change AtPI4K transcript levels to a great extent, indicating constitutive expression of the AtPI4K gene.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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