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Published on February 15, 2008; 10.1104/pp.108.116285

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Received January 12, 2008
Accepted February 11, 2008

Starch Biosynthetic Enzymes from Developing Zea mays Endosperm Associate in Multisubunit Complexes

Tracie A. Hennen-Bierwagen , Fushan Liu , Rebekah S. Marsh , Seungtaek Kim , Qinglei Gan , Ian J. Tetlow , Michael J. Emes , Martha G. James , and Alan M. Myers *

Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011; Department of Molecular and Cellular Biology, College of Biological Science, University of Guelph, Guelph, Ontario, N1G 2W1, Canada

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

Mutations affecting specific starch biosynthetic enzymes commonly have pleiotropic effects on other enzymes in the same metabolic pathway. Such genetic evidence indicates functional relationships between components of the starch biosynthetic system including starch synthases (SS), starch branching enzymes (BE), and starch debranching enzymes (DBE), however, the molecular explanation for these functional interactions is not known. One possibility is that specific SSs, BEs, and/or DBEs associate physically with each other in multisubunit complexes. To test this hypothesis, this study sought to identify stable associations between three separate SS polypeptides (SSI, SSIIa, SSIII) and three separate BE polypeptides (BEI, BEIIa, BEIIb) from maize amyloplasts. Detection methods included in vivo protein-protein interactions tests in yeast nuclei, immunoprecipitation, and affinity purification using recombinant proteins as the solid phase ligand. Eight different instances were detected of specific pairs of proteins associating either directly or indirectly in the same multi-subunit complex, and direct, pair-wise interactions were indicated the in vivo test in yeast. In addition, SSIIa, SSIII, BEIIa, and BEIIb all co-migrated in gel permeation chromatography (GPC) in a high molecular weight form of approximately 600 kDa, and SSIIa, BEIIa, and BEIIb also migrated in a second high molecular form, lacking SSIII, of approximately 300 kDa. Monomer forms of all these four proteins were also detected by GPC. The 600 kDa and 300 kDa complexes were stable at high salt concentration, suggesting that hydrophobic effects are involved in the association between subunits.




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