Identification of differential proteins of mungbean cotyledons during seed germination: a proteomic approach
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Proteomic analyses of seed germination, a complex physiological process is not yet explored in leguminous plants. Such study has been undertaken to reveal the variations that occur in cotyledonary proteins during seed gemination of mungbean (Vigna radiata L. Wilczek). Cotyledons were harvested for protein extraction and two dimensional gel electrophoreses at two developmental stages (I and II) of seed germination. Comparative qualitative and quantitative analyses between these two stages revealed differential expressions and de novo appearance or disappearance of proteins. Seventy-four proteins were identified by MALDI-TOF-MS and MS/MS and categorized according to their functions including metabolism and energy production, stress related, protein processing, transcription, storage etc. Majority of these proteins are associated with metabolisms indicating that cotyledons acquire an active metabolic state during seed germination. Many of the identified proteins were enzymes involved in starch and sucrose metabolism and those of glycolysis, tricarboxylic acid cycle etc. A pathway illustrating starch synthesis/breakdown, degradation of sucrose and the fates of reducing sugars in the germinating mungbean cotyledons has been elucidated. Predominance of antioxidant enzymes can be attributed to combat with reactive oxygen species generated due to active metabolism. Thus, the study comprehensively dealt with mechanisms of stored reserve mobilization and the roles of additional cotyledonary proteins of mungbean essential for successful seed germination and seedling development.
KeywordsCarbohydrate metabolism Cotyledonary proteins Seed germination MALDI-TOF-TOF Mungbean Proteomics
Authors are thankful to the Department of Science and Technology, Government of India (DST Sanction no. SR/SO/PS-58/05) for constant financial support in this area of research; and to the Director, Bose Institute for providing all infrastructural facilities and a Senior Research Fellowship to SG. The proteomic facilities provided by DST through IRHPA project (IR/SO/LF02/2002) are thankfully acknowledged.
- Arai M, Mori H, Imasek H (1991) Roles of sucrose-metabolizing enzymes in growth of seedlings: purification of acid invertase from growing hypocotyls of mung bean seedlings. Plant Cell Physiol 32:1291–1298Google Scholar
- Boudet J, Buitink J, Hoekstra FA, Rogniaux H, Larre C, Satour P, Leprince O (2006) Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance. Plant Physiol 140:1418–1436PubMedCentralPubMedCrossRefGoogle Scholar
- Finnie C, Maeda K, Østergaard O, Bak-Jensen KS, Larsen J, Svensson B (2004) Aspects of the barley seed proteome during development and germination. Prot Plant Proteins 32:517–519Google Scholar
- Fu X, Richards DE, Ait-ali T, Hynes LW, Ougham H, Peng J, Harberd NP (2002) Gibberellin-mediated proteasome-dependent degradation of the barley DELLA protein SLN1 repressor. Plant Cell 14:3191–3200Google Scholar
- Hedley CL (2001) Grain legume carbohydrates. In: Hedley CL (ed) Carbohydrates in grain legume seeds: improving nutritional quality and agronomic characteristics. CABI Publishing, New York, pp 2–14Google Scholar
- Maiti S, Chakraborty D, Kundu S, Paul S, Sengupta S, Pal A (2011) Developmentally regulated temporal expression and differential acid invertase activity in differentiating cotyledonary explants of mung bean [Vigna radiata (L.) Wilczek]. Plant Cell Tissue Organ Culture 107:417–425. doi: 10.1007/s11240-011-9992-9 CrossRefGoogle Scholar
- Mauseth JD (1998) Botany: an introduction to plant biology. Jones and Bartlett publishers, SudburyGoogle Scholar
- Ross HA, McRae D, Davies HV (1996) Sucrolytic enzyme activities in cotyledons of the faba bean. Plant Physiol 11:329–338Google Scholar
- Russel SD (1993) The egg cell: development and role in fertilization and early embryogenesis. Plant Cell 5:1349–1359Google Scholar
- Tsai YC, Wu MT, Hsieh JS, Hsing YIC, Shih MD (2008) Expression of Glycine max physiologically mature genes in soybean (Glycine max L.) tissues. J Genet Mol Biol 19:168–181Google Scholar