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Plant and Cell Physiology Advance Access originally published online on September 4, 2008
Plant and Cell Physiology 2008 49(10):1572-1579; doi:10.1093/pcp/pcn127
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© The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and the Japanese Society of Plant Physiologists are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

A Cell Wall-Bound Adenosine Nucleosidase is Involved in the Salvage of Extracellular ATP in Solanum tuberosum

David Riewe1, Lukasz Grosman1, Alisdair R. Fernie1, Henrik Zauber1, Cornelia Wucke1 and Peter Geigenberger1,2,*

1 Max-Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, D-14476 Potsdam-Golm, Germany
2 Leibniz-Institute of Vegetable and Ornamental Crops, Theodor-Echtermeyer-Weg 1, D-14979 Grossbeeren, Germany

*Corresponding author: E-mail, geigenberger{at}igzev.de; Fax, +49-33701-55391.


  Abstract

Extracellular ATP (eATP) has recently been demonstrated to play a crucial role in plant development and growth. To investigate the fate of eATP within the apoplast, we used intact potato (Solanum tuberosum) tuber slices as an experimental system enabling access to the apoplast without interference of cytosolic contamination. (i) Incubation of intact tuber slices with ATP led to the formation of ADP, AMP, adenosine, adenine and ribose, indicating operation of apyrase, 5'-nucleotidase and nucleosidase. (ii) Measurement of apyrase, 5'-nucleotidase and nucleosidase activities in fractionated tuber tissue confirmed the apoplastic localization for apyrase and phosphatase in potato and led to the identification of a novel cell wall-bound adenosine nucleosidase activity. (iii) When intact tuber slices were incubated with saturating concentrations of adenosine, the conversion of adenosine into adenine was much higher than adenosine import into the cell, suggesting a potential bypass of adenosine import. Consistent with this, import of radiolabeled adenine into tuber slices was inhibited when ATP, ADP or AMP were added to the slices. (iv) In wild-type plants, apyrase and adenosine nucleosidase activities were found to be co-regulated, indicating functional linkage of these enzymes in a shared pathway. (v) Moreover, adenosine nucleosidase activity was reduced in transgenic lines with strongly reduced apoplastic apyrase activity. When taken together, these results suggest that a complete ATP salvage pathway is present in the apoplast of plant cells.

Keywords: Adenosine nucleosidase - Apoplast - Apyrase - Cell wall - Extracellular ATP - Solanum tuberosum

Abbreviations: ANase, adenosine nucleosidase; CCCP, carbonyl cyanide m-chloro phenyl hydrazone; eATP, extracellular ATP; GC-MS, gas chromatography–mass spectrometry; UGPase, UDP-glucose pyrophosphorylase; PNP, p-nitrophenylphosphate; PUP, purine permease; RNAi, RNA interference.

(Received July 11, 2008; Accepted August 25, 2008)
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