Plant Physiol. Illumina
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First published online March 13, 2003; 10.1104/pp.102.016527

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Plant Physiol, May 2003, Vol. 132, pp. 137-145

STA11, a Chlamydomonas reinhardtii Locus Required for Normal Starch Granule Biogenesis, Encodes Disproportionating Enzyme. Further Evidence for a Function of alpha -1,4 Glucanotransferases during Starch Granule Biosynthesis in Green Algae1

Fabrice Wattebled, Jean-Philippe Ral, David Dauvillée, Alan M. Myers, Martha G. James, Ralf Schlichting, Christoph Giersch, Steven G. Ball, and Christophe D'Hulst*

Unité de Glycobiologie Structurale et Fonctionnelle, Unité Mixte de Recherche Centre National de la Recherche Scientifique/Université des Sciences et Technologies Lille 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve D'Ascq cedex, France (F.W., J.-P.R., D.D., S.B., C.D.H.); Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa 50011 (A.M., M.J.); and Institut für Botanik, Technische Universität, D-64287 Darmstadt, Germany (R.S., C.G.)

In Chlamydomonas reinhardtii, the presence of a defective STA11 locus results in significantly reduced granular starch deposition displaying major modifications in shape and structure. This defect simultaneously leads to the accumulation of linear malto-oligosaccharides (MOS). The mutants of STA11 were showed to lack D-enzyme, a plant alpha -1,4 glucanotransferase analogous to the Escherichia coli amylomaltase. We have cloned and characterized both the cDNA and gDNA corresponding to the C. reinhardtii D-enzyme. We now report allele-specific modifications of the D-enzyme gene in the mutants of STA11. These allele-specific modifications cosegregate with the corresponding sta11 mutations, thereby demonstrating that STA11 encodes D-enzyme. MOS production and starch accumulation were investigated during day and night cycles in wild-type and mutant C. reinhardtii cells. We demonstrate that in the algae MOS are produced during starch biosynthesis and degraded during the phases of net polysaccharide catabolism.

1 This work was supported by the Université des Sciences et Technologies de Lille, by the Ministère de l'Education Nationale et de la Recherche, by the Centre National de la Recherche Scientifique (Unité Mixte de Recherche 8576 du Centre National de la Recherche Scientifique), and by the Région Nord-Pas de Calais (fellowship no. 99060060 to F.W.).

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

© 2003 American Society of Plant Biologists


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