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Plant and Cell Physiology Advance Access originally published online on June 13, 2006
Plant and Cell Physiology 2006 47(7):926-934; doi:10.1093/pcp/pcj065
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© The Author 2006. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Cloning, Expression and Characterization of a Nudix Hydrolase that Catalyzes the Hydrolytic Breakdown of ADP-glucose Linked to Starch Biosynthesis in Arabidopsis thaliana

Francisco José Muñoz1,*, Edurne Baroja-Fernández1, María Teresa Morán-Zorzano, Nora Alonso-Casajús and Javier Pozueta-Romero*

Instituto de Agrobiotecnología, Universidad Pública de Navarra/Consejo Superior de Investigaciones Científicas/Gobierno de Navarra, Ctra. Mutilva s/n, 31192 Mutilva Baja, Navarra, Spain

* Corresponding authors: Javier Pozueta-Romero, E-mail, javier.pozueta{at}unavarra.es; Fax, +34-948232191; Francisco José Muñoz, E-mail, francisco.munoz{at}unavarra.es; Fax, +34-948232191.

‘Nudix’ hydrolases are widely distributed nucleotide pyrophosphatases that possess a conserved GX5EX7REUXEEXGU motif where U is usually isoleucine, leucine or valine. Among them, Escherichia coli ADP-sugar pyrophosphatase (ASPP) has been shown to catalyze the hydrolytic breakdown of ADP-glucose linked to bacterial glycogen biosynthesis. Comparisons of the 31 different Nudix-encoding sequences of the Arabidopsis genome with those coding for known bacterial and mammalian ASPPs identified one sequence possessing important divergences in the Nudix motif that, once expressed in E. coli, produced a protein with ASPP activity. This protein, designated as AtASPP, shares strong homology with hypothetical rice and potato proteins, indicating that ASPPs are widely distributed in both mono- and dicotyledonous plants. As a first step to test the possible involvement of plant ASPPs in regulating the intracellular levels of ADP-glucose linked to starch biosynthesis, we produced and characterized AtASPP-overexpressing Arabidopsis plants. Source leaves from these plants exhibited a large reduction in the levels of both ADP-glucose and starch, indicating that plant ASPPs catalyze the hydrolytic breakdown of a sizable pool of ADP-glucose linked to starch biosynthesis. No pleiotropic changes in maximum catalytic activities of enzymes closely linked to starch metabolism could be detected in AtASPP-overexpressing leaves. The overall information provides the first evidence for the existence of plant Nudix hydrolases that have access to an intracellular pool of ADP-glucose linked to starch biosynthesis.

1 These authors contributed equally to this work.

The nucleotide sequences of AtASPP and StASPP encoding cDNAs have been submitted to EMBL database under accession numbers AJ748742 and AM180509, respectively.

(Received April 6, 2006; Accepted May 19, 2006)
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