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DEVELOPMENT AND HORMONE ACTION

Developmental Analysis of Maize Endosperm Proteome Suggests a Pivotal Role for Pyruvate Orthophosphate Dikinase^1,[W],[OA]

Unité Mixte de Recherche 206, Chimie Biologique, Institut National de la Recherche Agronomique, Institut National Agronomique Paris-Grignon, F–78850 Thiverval Grignon, France (V.M.); Laboratoire Biotechnologie des Plantes, Unité Mixte de Recherche 8618, Université Paris Sud, F–91405 Orsay, France (C.T., J.-L.P.); Centre National de la Recherche Scientifique, F–91405 Orsay, France (C.T., J.-L.P.); and Unité Mixte de Recherche 8120, Institut National de la Recherche Agronomique, Université Paris Sud, Centre National de la Recherche Scientifique, Institut National Agronomique Paris-Grignon, F–91190 Gif sur Yvette, France (M.L.G., C.D.)

Although the morphological steps of maize (Zea mays) endosperm development are well described, very little is known concerning the coordinated accumulation of the numerous proteins involved. Here, we present a proteomic study of maize endosperm development. The accumulation pattern of 409 proteins at seven developmental stages was examined. Hierarchical clustering analysis allowed four main developmental profiles to be recognized. Comprehensive investigation of the functions associated with clusters resulted in a consistent picture of the developmental coordination of cellular processes. Early stages, devoted to cellularization, cell division, and cell wall deposition, corresponded to maximal expression of actin, tubulins, and cell organization proteins, of respiration metabolism (glycolysis and tricarboxylic acid cycle), and of protection against reactive oxygen species. An important protein turnover, which is likely associated with the switch from growth and differentiation to storage, was also suggested from the high amount of proteases. A relative increase of abundance of the glycolytic enzymes compared to tricarboxylic acid enzymes is consistent with the recent demonstration of anoxic conditions during starch accumulation in the endosperm. The specific late-stage accumulation of the pyruvate orthophosphate dikinase may suggest a critical role of this enzyme in the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance.

The authors responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) are: Valérie Méchin (mechin{at}grignon.inra.fr) and Catherine Damerval (damerval{at}moulon.inra.fr).

^[W] The online version of this article contains Web-only data.

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www.plantphysiol.org/cgi/doi/10.1104/pp.106.092148

^* Corresponding author; e-mail mechin{at}grignon.inra.fr; fax 33–1–30–81–53–73.

Received November 7, 2006; accepted January 9, 2007; published January 19, 2007.

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