Proteome-wide characterization of sugarbeet seed vigor and its tissue specific expression.
Proteomic analysis of mature sugarbeet seeds led to the identification of 759 proteins and their specific tissue expression in root, cotyledons, and perisperm. In particular, the proteome of the perispermic storage tissue found in many seeds of the Caryophyllales is described here. The data allowed us to reconstruct in detail the metabolism of the seeds toward recapitulating facets of seed development and provided insights into complex behaviors such as germination. The seed appears to be well prepared to mobilize the major classes of reserves (the proteins, triglycerides, phytate, and starch) during germination, indicating that the preparation of the seed for germination is mainly achieved during its maturation on the mother plant. Furthermore, the data revealed several pathways that can contribute to seed vigor, an important agronomic trait defined as the potential to produce vigorous seedlings, such as glycine betaine accumulation in seeds. This study also identified several proteins that, to our knowledge, have not previously been described in seeds. For example, the data revealed that the sugarbeet seed can initiate translation either through the traditional cap-dependent mechanism or by a cap-independent process. The study of the tissue specificity of the seed proteome demonstrated a compartmentalization of metabolic activity between the roots, cotyledons, and perisperm, indicating a division of metabolic tasks between the various tissues. Furthermore, the perisperm, although it is known as a dead tissue, appears to be very active biochemically, playing multiple roles in distributing sugars and various metabolites to other tissues of the embryo.
Catusse
Julie
J
Centre National de la Recherche Scientifique-Université Claude Bernard Lyon 1, Institut National des Sciences Appliquées-Bayer CropScience Joint Laboratory, Unité Mixte de Recherche 5240, Bayer CropScience, 14-20 rue Pierre Baizet, Lyon Cedex 9, France.
Strub
Jean-Marc
JM
Job
Claudette
C
Van Dorsselaer
Alain
A
Job
Dominique
D
D000596:Amino Acids / Q000096:biosynthesis; D027461:Beta vulgaris / Q000235:genetics / Q000378:metabolism*; D001622:Betaine / Q000378:metabolism; D019663:Chenopodiaceae / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D006038:Glyoxylates / Q000378:metabolism; D045782:Hemiterpenes / Q000096:biosynthesis; D053858:Metabolic Networks and Pathways; D008954:Models, Biological; D009943:Organophosphorus Compounds; D010442:Peptide Chain Initiation, Translational; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism; D020543:Proteome; D012639:Seeds / Q000235:genetics / Q000378:metabolism; D014018:Tissue Distribution
D000596:Amino Acids; D006038:Glyoxylates; D045782:Hemiterpenes; D009943:Organophosphorus Compounds; D010940:Plant Proteins; D020543:Proteome; C004809:isopentenyl pyrophosphate; D001622:Betaine; C031150:glyoxylic acid