Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase
- Streb, Sebastian Institute of Plant Sciences, ETH Zurich, Switzerland
- Delatte, Thierry Institute of Plant Sciences, ETH Zurich, Switzerland
- Umhang, Martin Institute of Plant Sciences, ETH Zurich, Switzerland
- Eicke, Simona Institute of Plant Sciences, ETH Zurich, Switzerland
- Schorderet, Martine Department of Plant Biology, University of Fribourg, Switzerland
- Reinhardt, Didier Department of Plant Biology, University of Fribourg, Switzerland
- Zeeman, Samuel C. Institute of Plant Sciences, ETH Zurich, Switzerland
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12.12.2008
Published in:
- The Plant Cell. - 2009, vol. 20, p. 3448-3466
English
Several studies have suggested that debranching enzymes (DBEs) are involved in the biosynthesis of amylopectin, the major constituent of starch granules. Our systematic analysis of all DBE mutants of Arabidopsis thaliana demonstrates that when any DBE activity remains, starch granules are still synthesized, albeit with altered amylopectin structure. Quadruple mutants lacking all four DBE proteins (Isoamylase1 [ISA1], ISA2, and ISA3, and Limit-Dextrinase) are devoid of starch granules and instead accumulate highly branched glucans, distinct from amylopectin and from previously described phytoglycogen. A fraction of these glucans are present as discrete, insoluble, nanometer-scale particles, but the structure and properties of this material are radically altered compared with wild-type amylopectin. Superficially, these data support the hypothesis that debranching is required for amylopectin synthesis. However, our analyses show that soluble glucans in the quadruple DBE mutant are degraded by {alpha}- and β-amylases during periods of net accumulation, giving rise to maltose and branched malto-oligosaccharides. The additional loss of the chloroplastic {alpha}-amylase AMY3 partially reverts the phenotype of the quadruple DBE mutant, restoring starch granule biosynthesis. We propose that DBEs function in normal amylopectin synthesis by promoting amylopectin crystallization but conclude that they are not mandatory for starch granule synthesis.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 12216
- DOI 10.1105/tpc.108.063487
- Persistent URL
- https://folia.unifr.ch/unifr/documents/301135
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