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Plant Physiol, June 2001, Vol. 126, pp. 801-810
Molecular Characterization of At5PTase1, an Inositol Phosphatase
Capable of Terminating Inositol Trisphosphate
Signaling1,[w]
Sara E.
Berdy,
Joerg
Kudla,2
Wilhelm
Gruissem, and
Glenda E.
Gillaspy*
Department of Biochemistry and Fralin Biotechnology Center,
Virginia Polytechnic Institute and State University, Blacksburg,
Virginia 24061 (S.E.B., J.K., G.E.G.); and Department of Plant and
Microbial Biology, University of California, Berkeley, California 94702 (W.G.)
The inositol triphosphate (IP3)-signaling pathway has
been associated with several developmental and physiological processes in plants, but we currently know little about the regulation of this
pathway. Inositol 5' phosphatases (5PTases) are enzymes that remove a
5' phosphate from several potential second messengers, including
IP3. In catalyzing the removal of a 5' phosphate from second messenger substrates, 5PTases can act to terminate signal transduction events. We describe the molecular analysis of At5PTase1, a
5PTase gene from Arabidopsis. When expressed transiently in Arabidopsis
leaf tissue or ectopically in transgenic plants, At5PTase1 allowed for
the increased hydrolysis of I(1,4,5)P3 and
I(1,3,4,5)P4 substrates. At5PTase1 did not hydrolyze I(1)P,
I(1,4)P2, or PI(4,5)P2 substrates. This
substrate specificity was similar to that of the human Type I 5PTase.
We identified 14 other potential At5PTase genes and constructed an
unrooted phylogenetic tree containing putative Arabidopsis, human, and
yeast 5PTase proteins. This analysis indicated that the Arabidopsis
5PTases were grouped in two separate branches of the tree. The
multiplicity of At5PTases indicates that these enzymes may have
different substrate specificities and play different roles in signal
termination in Arabidopsis.
1
This work was supported by a Jeffress Trust
(award to G.E.G.) and by the Hatch Project (no. VA-135583).
2
Present Address: Allgemeine Botanik, Universität
Ulm, 89069 Ulm, Germany.
[w]
The online version of this article contains Web-only
data. The supplemental material is available at
www.plantphysiol.org.
*
Corresponding author; e-mail gillaspy{at}vt.edu; fax 540-231-1850.
© 2001 American Society of Plant Physiologists
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