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Apyrase Functions in Plant Phosphate Nutrition and Mobilizes Phosphate from Extracellular ATP1

Collin Thomas, Yu Sun, Katie Naus, Alan Lloyd, and Stanley Roux*

Botany Department and the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78713

ATP, which is present in the extracellular matrix of multicellular organisms and in the extracellular fluid of unicellular organisms, has been shown to function as a signaling molecule in animals. The concentration of extracellular ATP (xATP) is known to be functionally modulated in part by ectoapyrases, membrane-associated proteins that cleave the gamma - and beta -phosphates on xATP. We present data showing a previously unreported (to our knowledge) linkage between apyrase and phosphate transport. An apyrase from pea (Pisum sativum) complements a yeast (Saccharomyces cerevisiae) phosphate-transport mutant and significantly increases the amount of phosphate taken up by transgenic plants overexpressing the gene. The transgenic plants show enhanced growth and augmented phosphate transport when the additional phosphate is supplied as inorganic phosphate or as ATP. When scavenging phosphate from xATP, apyrase mobilizes the gamma -phosphate without promoting the transport of the purine or the ribose.


1   This work was supported by grants from the National Science Foundation and the National Aeronautics and Space Administration and by a National Science Foundation graduate fellowship to C.T.
*   Corresponding author; e-mail sroux{at}uts.cc.utexas.edu; fax 1-512-471-3878.

Plant Physiol. (1999) 119: 543-552
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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