Abstract
Seed storage proteins play a fundamental role in plant reproduction and human nutrition. They accumulate during seed development as reserve material for germination and seedling growth and are a major source of dietary protein for human consumption. Storage proteins encompass multiple isoforms encoded by multi-gene families that undergo abundant glycosylations and phosphorylations. Two-dimensional electrophoresis (2-DE) is a proteomic tool especially suitable for the characterization of storage proteins because of their peculiar characteristics. In particular, storage proteins are soluble multimeric proteins highly represented in the seed proteome that contain polypeptides of molecular mass between 10 and 130 kDa. In addition, high-resolution profiles can be achieved by applying targeted 2-DE protocols. 2-DE coupled with mass spectrometry (MS) has traditionally been the methodology of choice in numerous studies on the biology of storage proteins in a wide diversity of plants. 2-DE-based reference maps have decisively contributed to the current state of our knowledge about storage proteins in multiple key aspects, including identification of isoforms and quantification of their relative abundance, identification of phosphorylated isoforms and assessment of their phosphorylation status, and dynamic changes of isoforms during seed development and germination both qualitatively and quantitatively. These advances have translated into relevant information about meaningful traits in seed breeding such as protein quality, longevity, gluten and allergen content, stress response and antifungal, antibacterial, and insect susceptibility. This review addresses progress on the biology of storage proteins and application areas in seed breeding using 2-DE-based maps.
Highlights
Storage proteins accumulate during seed development within membrane-bound organelles called protein bodies and serve as a reservoir of amino acids, reduced nitrogen, carbon, and sulfur required for germinating seedlings [1,2,3,4,5]
2-DE can be routinely applied for the separation of highly complex mixtures of proteins from cell, tissue, organ and organism protein extracts in accordance with their isoelectric point and molecular mass (Mr ) in two successive steps: isoelectric focusing (IEF) in the first dimension and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) to resolve denatured proteins in the second
This review shows that the use of 2-DE combined with mass spectrometry (MS) is of vital importance to advancing the knowledge of the isoforms of storage proteins and their dynamic changes during seed development and germination in a wide diversity of plants, and in relevant fields closely connected to seed breeding
Summary
Storage proteins accumulate during seed development within membrane-bound organelles called protein bodies and serve as a reservoir of amino acids, reduced nitrogen, carbon, and sulfur required for germinating seedlings [1,2,3,4,5]. A minority of studies used 2-DE specific protocols aimed at obtaining high-resolution profiles of storage proteins [29,30,42,43,44] This approach is very useful to characterize storage protein isoforms and their response to internal and external seed stimuli at higher level of resolution, the information it provides is decoupled from the rest of seed proteins. The application of these two strategies has provided most of the advances in the biology of storage proteins These advances cover facets as diverse as the identification of isoforms and their relative abundance, the identification, mapping and quantitation of phosphorylated and glycosylated isoforms and the assessment of qualitative and quantitative changes of isoforms during seed development and germination. This review focuses on the use and importance of 2-DE-based maps to obtain insights into the biology of storage proteins and application areas in seed breeding
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