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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 - and
-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 -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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