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First published online April 22, 2005; 10.1104/pp.105.059295

Plant Physiology 138:184-195 (2005)
© 2005 American Society of Plant Biologists

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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Mutants of Arabidopsis Lacking a Chloroplastic Isoamylase Accumulate Phytoglycogen and an Abnormal Form of Amylopectin1,[w]

Fabrice Wattebled2, Ying Dong2, Sylvain Dumez, David Delvallé, Véronique Planchot, Pierre Berbezy, Darshna Vyas, Paul Colonna, Manash Chatterjee3, Steven Ball and Christophe D'Hulst*

Unité de Glycobiologie Structurale et Fonctionnelle, Unité Mixte de Recherche 8576 Centre National de la Recherche Scientifique, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (F.W., Y.D., S.D., D.D., S.B., C.D.); Unité de Recherche sur les Biopolymères, Intéractions et Assemblages, Institut National de la Recherche Agronomique Centre de Nantes, 44316 Nantes cedex 3, France (V.P., P.C.); and Biogemma UK Ltd, Cambridge CB4 0GZ, United Kingdom (P.B., D.V., M.C.)

Mutant lines defective for each of the four starch debranching enzyme (DBE) genes (AtISA1, AtISA2, AtISA3, and AtPU1) detected in the nuclear genome of Arabidopsis (Arabidopsis thaliana) were produced and analyzed. Our results indicate that both AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of DBE named Iso1, the major isoamylase activity found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content in both lines and to the accumulation of water-soluble polysaccharides whose structure is similar to glycogen. In addition, the residual amylopectin structure in the corresponding mutant lines displays a strong modification when compared to the wild type, suggesting a direct, rather than an indirect, function of Iso1 during the synthesis of amylopectin. Mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure. This result suggests that this isoamylase-type of DBE plays a major role during starch mobilization. The analysis of the Atpu1 single-mutant lines did not lead to a distinctive phenotype. However, Atisa2/Atpu1 double-mutant lines display a 92% decrease in starch content. This suggests that the function of pullulanase partly overlaps that of Iso1, although its implication remains negligible when Iso1 is present within the cell.

1 This work was supported by Génoplante (project no. Af2001030), by the Région Nord Pas de Calais, by the Ministère Délégué à la Recherche (Action Concertée Incitative Jeunes-Chercheurs no. JC5145), by the European Community (Feder, CPER2000–2006), and by the Centre National de la Recherche Scientifique.

2 These authors contributed equally to the paper.

3 Present address: National Institute of Agricultural Biology, Hintingdon Road, Cambridge CB3 0LE, UK.

[w] The online version of this article contains Web-only data.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.059295.

* Corresponding author; e-mail christophe.dhulst{at}univ-lille1.fr; fax 33–3–20–43–65–55.

Received January 26, 2005; returned for revision March 1, 2005; accepted March 3, 2005.




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