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Mutants of Arabidopsis Lacking Starch Branching Enzyme II Substitute Plastidial Starch Synthesis by Cytoplasmic Maltose Accumulation^[W]

^a 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
^b Unité de Recherche Biopolymères, Interactions, Assemblages, Centre de Nantes, Institut National de la Recherche Agronomique, 44316 Nantes Cedex 3, France

² To whom correspondence should be addressed. E-mail christophe.dhulst{at}univ-lille1.fr; fax 33-3-20-43-6555.

Three genes, BE1, BE2, and BE3, which potentially encode isoforms of starch branching enzymes, have been found in the genome of Arabidopsis thaliana. Although no impact on starch structure was observed in null be1 mutants, modifications in amylopectin structure analogous to those of other branching enzyme II mutants were detected in be2 and be3. No impact on starch content was found in any of the single mutant lines. Moreover, three double mutant combinations were produced (be1 be2, be1 be3, and be2 be3), and the impact of the mutations on starch content and structure was analyzed. Our results suggest that BE1 has no apparent function for the synthesis of starch in the leaves, as both be1 be2 and be1 be3 double mutants display the same phenotype as be2 and be3 separately. However, starch synthesis was abolished in be2 be3, while high levels of -maltose were assayed in the cytosol. This result indicates that the functions of both BE2 and BE3, which belong to class II starch branching enzymes, are largely redundant in Arabidopsis. Moreover, we demonstrate that maltose accumulation depends on the presence of an active ADP-glucose pyrophosphorylase and that the cytosolic transglucosidase DISPROPORTIONATING ENZYME2, required for maltose metabolization, is specific for ß-maltose.

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