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Published on May 14, 2008; 10.1104/pp.108.117564

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Received February 7, 2008
Accepted May 12, 2008

The potato-specific apyrase is apoplastically localized and has influence on gene expression, growth and development

David Riewe , Lukasz Grosman , Alisdair R. Fernie , Cornelia Wucke , and Peter Geigenberger *

Max-Planck Institute of Molecular Plant Physiology, Am Muhlenberg 1, 14476 Potsdam-Golm, Germany

* Corresponding author; email: geigenberger{at}mpimp-golm.mpg.de.

Apyrases hydrolyze nucleoside triphosphates and diphosphates and are found in all eukaryotes and a few prokaryotes. Although their enzymatic properties have been well characterized, relatively little is known regarding their subcellular localization and physiological function in plants. In the present study we used reverse genetic and biochemical approaches to investigate the role of potato-specific apyrase. Silencing of the apyrase gene family with RNAi-constructs under the control of the constitutive 35S-promoter led to a strong decrease in apyrase activity to below 10% of the wild-type level. This decreased activity led to phenotypic changes in the transgenic lines including a general retardation in growth, an increase in tuber number per plant and differences in tuber morphology. Silencing of apyrase under the control of a tuber-specific promoter led to similar changes in tuber morphology, however, there were no direct effects of apyrase inhibition on tuber metabolism. DNA micro-arrays revealed that decreased expression of apyrase leads to increased levels of transcripts coding for cell wall proteins involved in growth and genes involved in energy transfer and starch synthesis. To place these results in context, we determined the subcellular localization of the potato-specific apyrase. Using a combination of approaches we were able to demonstrate that this enzyme is localized to the apoplast. We describe the evidence which underlies both this fact and that potato-specific apyrase has a crucial role in regulating growth and development.






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