Proteome and phosphoproteome analysis of starch granule-associated proteins from normal maize and mutants affected in starch biosynthesis

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 sta...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 59(2008), 12 vom: 15., Seite 3395-406
1. Verfasser: Grimaud, Florent (VerfasserIn)
Weitere Verfasser: Rogniaux, Hélène, James, Martha G, Myers, Alan M, Planchot, Véronique
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2008
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Plant Proteins Starch 9005-25-8 Starch Phosphorylase EC 2.4.1.- 1,4-alpha-Glucan Branching Enzyme EC 2.4.1.18 mehr... Starch Synthase EC 2.4.1.21
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100 1 |a Grimaud, Florent  |e verfasserin  |4 aut 
245 1 0 |a Proteome and phosphoproteome analysis of starch granule-associated proteins from normal maize and mutants affected in starch biosynthesis 
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520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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650 7 |a Starch  |2 NLM 
650 7 |a 9005-25-8  |2 NLM 
650 7 |a Starch Phosphorylase  |2 NLM 
650 7 |a EC 2.4.1.-  |2 NLM 
650 7 |a 1,4-alpha-Glucan Branching Enzyme  |2 NLM 
650 7 |a EC 2.4.1.18  |2 NLM 
650 7 |a Starch Synthase  |2 NLM 
650 7 |a EC 2.4.1.21  |2 NLM 
700 1 |a Rogniaux, Hélène  |e verfasserin  |4 aut 
700 1 |a James, Martha G  |e verfasserin  |4 aut 
700 1 |a Myers, Alan M  |e verfasserin  |4 aut 
700 1 |a Planchot, Véronique  |e verfasserin  |4 aut 
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