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Published on January 23, 2009; 10.1104/pp.109.135293

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Received January 7, 2009
Accepted January 19, 2009

Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts

Tracie A. Hennen-Bierwagen , Qiaohui Lin , Florent Grimaud , Veronique Planchot , Peter L. Keeling , Martha G. James , and Alan M. Myers *

Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011; Institut National de la Recherche Agronomique, Unite de Recherche Biopolymeres, Interactions, Assemblages, BP 71627, F-44316 Nantes Cedex 03, France

* Corresponding author; email: ammyers{at}iastate.edu.

Starch biosynthetic enzymes from maize and wheat amyloplasts exist in cell extracts in high molecular weight complexes, however, the nature of those assemblies remains to be defined. This study tested interdependence of the maize enzymes starch synthase IIa (SSIIa), SSIII, starch branching enzyme IIb (SBEIIb), and SBEIIa for assembly into multi-subunit complexes. Mutations that eliminated any one of those proteins also prevented the others from assembling into a high molecular form of approximately 670 kDa, so that SSIII, SSIIa, SBEIIa, and SBEIIb most likely all exist together in the same complex. SSIIa, SBEIIb, and SBEIIa, but not SSIII, were also interdependent for assembly into a complex of approximately 300 kDa. SSIII, SSIIa, SBEIIa, and SBEIIb co-purified through successive chromatography steps, and SBEIIa, SBEIIb, and SSIIa co-immunoprecipitated with SSIII in a phosphorylation-dependent manner. SBEIIa and SBEIIb also were retained on an affinity column bearing a specific conserved fragment of SSIII located outside of the SS catalytic domain. Additional proteins that co-purified with SSIII in multiple biochemical methods included the two known isoforms of pyruvate orthophosphate dikinase (PPDK), large and small subunits of ADP glucose pyrophosphorylase, and the sucrose synthase isoform SUS-SH1. PPDK and SUS-SH1 required SSIII, SSIIa, SBEIIa, and SBEIIb for assembly into the 670 kDa complex. These complexes may function in global regulation of carbon partitioning between metabolic pathways in developing seeds.




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F. Liu, A. Makhmoudova, E. A. Lee, R. Wait, M. J. Emes, and I. J. Tetlow
The amylose extender mutant of maize conditions novel protein-protein interactions between starch biosynthetic enzymes in amyloplasts
J. Exp. Bot., November 1, 2009; 60(15): 4423 - 4440.
[Abstract] [Full Text] [PDF]


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