Identification of Early Represented Gluten Proteins during Durum Wheat Grain Development

The time course of biosynthesis and accumulation of storage proteins in developing grains of durum wheat (Triticum turgidum ssp. durum (Desf.) Husn.) pasta-quality reference cv. Svevo was investigated at the protein level for the first time. Seeds were harvested at key kernel developmental stages, n...

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Veröffentlicht in:Journal of agricultural and food chemistry 2017-04, Vol.65 (15), p.3242-3250
Hauptverfasser: Mazzeo, Maria Fiorella, Di Stasio, Luigia, D’Ambrosio, Chiara, Arena, Simona, Scaloni, Andrea, Corneti, Simona, Ceriotti, Aldo, Tuberosa, Roberto, Siciliano, Rosa Anna, Picariello, Gianluca, Mamone, Gianfranco
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container_end_page 3250
container_issue 15
container_start_page 3242
container_title Journal of agricultural and food chemistry
container_volume 65
creator Mazzeo, Maria Fiorella
Di Stasio, Luigia
D’Ambrosio, Chiara
Arena, Simona
Scaloni, Andrea
Corneti, Simona
Ceriotti, Aldo
Tuberosa, Roberto
Siciliano, Rosa Anna
Picariello, Gianluca
Mamone, Gianfranco
description The time course of biosynthesis and accumulation of storage proteins in developing grains of durum wheat (Triticum turgidum ssp. durum (Desf.) Husn.) pasta-quality reference cv. Svevo was investigated at the protein level for the first time. Seeds were harvested at key kernel developmental stages, namely, 3 (seed increase 3-fold in size), 5 (kernel development, water-ripe stage), 11 (kernel development, water-ripe stage), 16 (kernel full development, water-ripe stage), 21 (milk-ripe stage), and 30 (dough stage) days postanthesis (dpa). Gliadins and glutenins were fractionated according to their different solubility and individually analyzed after fractionation by reversed-phase high performance liquid chromatography and sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Proteins were identified by liquid chromatography–tandem mass spectrometry of proteolytic peptides. The α- and γ-gliadin were already detected at 3 dpa. The biosynthesis of high molecular mass glutenin Bx7 was slightly delayed (11 dpa). Most of the gluten proteins accumulated rapidly between 11 and 21 dpa, with a minor further increase up to 30 dpa. The expression pattern of gluten proteins in Triticum durum at the early stages of synthesis provides reference data sets for future applications in crop breeding and growth monitoring.
doi_str_mv 10.1021/acs.jafc.7b00571
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Agric. Food Chem</addtitle><description>The time course of biosynthesis and accumulation of storage proteins in developing grains of durum wheat (Triticum turgidum ssp. durum (Desf.) Husn.) pasta-quality reference cv. Svevo was investigated at the protein level for the first time. Seeds were harvested at key kernel developmental stages, namely, 3 (seed increase 3-fold in size), 5 (kernel development, water-ripe stage), 11 (kernel development, water-ripe stage), 16 (kernel full development, water-ripe stage), 21 (milk-ripe stage), and 30 (dough stage) days postanthesis (dpa). Gliadins and glutenins were fractionated according to their different solubility and individually analyzed after fractionation by reversed-phase high performance liquid chromatography and sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Proteins were identified by liquid chromatography–tandem mass spectrometry of proteolytic peptides. The α- and γ-gliadin were already detected at 3 dpa. The biosynthesis of high molecular mass glutenin Bx7 was slightly delayed (11 dpa). Most of the gluten proteins accumulated rapidly between 11 and 21 dpa, with a minor further increase up to 30 dpa. 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subjects Electrophoresis, Polyacrylamide Gel
Glutens - chemistry
Glutens - metabolism
Molecular Weight
Seeds - chemistry
Seeds - growth & development
Seeds - metabolism
Triticum - chemistry
Triticum - growth & development
Triticum - metabolism
title Identification of Early Represented Gluten Proteins during Durum Wheat Grain Development
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