Proteome and phosphoproteome analysis of starch granule-associated proteins from normal maize and mutants affected in starch biosynthesis
Autor: | Martha G. James, Alan M. Myers, Véronique Planchot, Florent Grimaud, Hélène Rogniaux |
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Přispěvatelé: | Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University (ISU) |
Jazyk: | angličtina |
Rok vydání: | 2008 |
Předmět: |
0106 biological sciences
Proteomics Physiology Starch Mutant Plant Science Biology 01 natural sciences Zea mays Endosperm 03 medical and health sciences chemistry.chemical_compound Protein phosphorylation Starch Synthase 1 4-alpha-Glucan Branching Enzyme Phosphorylation 030304 developmental biology Plant Proteins 2. Zero hunger 0303 health sciences Starch phosphorylase Granule (cell biology) food and beverages Starch Phosphorylase starch biosynthesis [SDV.BV.BOT]Life Sciences [q-bio]/Vegetal Biology/Botanics Research Papers chemistry Biochemistry Amylopectin Proteome Mutation biology.protein Starch synthase starch granules 010606 plant biology & botany |
Zdroj: | Journal of Experimental Botany Journal of Experimental Botany, Oxford University Press (OUP), 2008, 59 (12), pp.3395-3406. ⟨10.1093/jxb/ern198⟩ |
ISSN: | 1460-2431 0022-0957 |
Popis: | International audience; In addition to the exclusively granule-bound starch synthase GBSSI, starch granules also bind significant proportions of other starch biosynthetic enzymes, particularly starch synthases (SS) SSI and SSIIa, and starch branching enzyme (BE) BEIIb. Whether this association is a functional aspect of starch biosynthesis, or results from non-specific entrapment during amylopectin crystallization, is not known. This study utilized genetic, immunological, and proteomic approaches to investigate comprehensively the proteome and phosphoproteome of Zea mays endosperm starch granules. SSIII, BEI, BEIIa, and starch phosphorylase were identified as internal granule-associated proteins in maize endosperm, along with the previously identified proteins GBSS, SSI, SSIIa, and BEIIb. Genetic analyses revealed three instances in which granule association of one protein is affected by the absence of another biosynthetic enzyme. First, eliminating SSIIa caused reduced granule association of SSI and BEIIb, without affecting GBSS abundance. Second, eliminating SSIII caused the appearance of two distinct electrophoretic mobility forms of BEIIb, whereas only a single migration form of BEIIb was observed in wild type or any other mutant granules examined. Third, eliminating BEIIb caused significant increases in the abundance of BEI, BEIIa, SSIII, and starch phosphorylase in the granule, without affecting SSI or SSIIa. Analysis of the granule phosphoproteome with a phosphorylation-specific dye indicated that GBSS, BEIIb, and starch phosphorylase are all phosphorylated as they occur in the granule. These results suggest the possibility that starch metabolic enzymes located in granules are regulated by post-translational modification and/or protein-protein interactions. |
Databáze: | OpenAIRE |
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