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A role for seed storage proteins in Arabidopsis seed longevity.

Nguyen TP, Cueff G, Hegedus DD, Rajjou L, Bentsink L - J. Exp. Bot. (2015)

Bottom Line: Proteomics approaches have been a useful tool for determining the biological roles and functions of individual proteins and identifying the molecular mechanisms that govern seed germination, vigour and viability in response to ageing.Results confirmed the role of antioxidant systems, notably vitamin E, and indicated that protection and maintenance of the translation machinery and energy pathways are essential for seed longevity.Cruciferins (CRUs) are the most abundant SSPs in Arabidopsis and seeds of a triple mutant for three CRU isoforms (crua crub cruc) were more sensitive to artificial ageing and their seed proteins were highly oxidized compared with wild-type seeds.

View Article: PubMed Central - PubMed

Affiliation: Wageningen Seed Lab, Laboratory of Plant Physiology, Wageningen University, 6708 PB Wageningen, The Netherlands Department of Molecular Plant Physiology, Utrecht University, 3584 CH Utrecht, The Netherlands.

No MeSH data available.


Protein carbonylation of seed proteins in after-ripened (AR) artificially aged seeds (Aged). (A) 1D gel electrophoresis stained with Coomassie Brilliant Blue of total seed protein extracts from Col, the triple cruciferin mutant abc (crua crub cruc) and the napin mutant (RNAi-napin). (B) Carbonylated proteins as detected by immunodetection of protein-bound DNP after derivatization with hydrazine.
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Figure 6: Protein carbonylation of seed proteins in after-ripened (AR) artificially aged seeds (Aged). (A) 1D gel electrophoresis stained with Coomassie Brilliant Blue of total seed protein extracts from Col, the triple cruciferin mutant abc (crua crub cruc) and the napin mutant (RNAi-napin). (B) Carbonylated proteins as detected by immunodetection of protein-bound DNP after derivatization with hydrazine.

Mentions: 1D-PAGE analysis of total protein extracts confirmed the reduction of cruciferin and napin proteins in dry seeds of the crua crub cruc and RNAi-napin mutant, respectively (Fig. 6A). Carbonylation of seed proteins was significant in both AR and aged seeds, with cruciferin being a major target in the wild-type and RNAi-napin lines (Fig. 6B). The cruciferin mutant exhibited a different protein carbonylation pattern in which carbonylation levels increased for the remaining proteins compared to the wild-type profile. In addition, there is a slight reduction in protein oxidation profiles comparing aged to AR seeds of all three genotypes, but also this effect was the strongest in the crua crub cruc mutant. Our result provides the first proof that SSPs, mainly cruciferins, are buffers for oxidative stress especially in dry seeds during storage. The carbonylated proteins in SSP mutants are interesting, since they will reveal new insights on the elements important for seed longevity.


A role for seed storage proteins in Arabidopsis seed longevity.

Nguyen TP, Cueff G, Hegedus DD, Rajjou L, Bentsink L - J. Exp. Bot. (2015)

Protein carbonylation of seed proteins in after-ripened (AR) artificially aged seeds (Aged). (A) 1D gel electrophoresis stained with Coomassie Brilliant Blue of total seed protein extracts from Col, the triple cruciferin mutant abc (crua crub cruc) and the napin mutant (RNAi-napin). (B) Carbonylated proteins as detected by immunodetection of protein-bound DNP after derivatization with hydrazine.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4588887&req=5

Figure 6: Protein carbonylation of seed proteins in after-ripened (AR) artificially aged seeds (Aged). (A) 1D gel electrophoresis stained with Coomassie Brilliant Blue of total seed protein extracts from Col, the triple cruciferin mutant abc (crua crub cruc) and the napin mutant (RNAi-napin). (B) Carbonylated proteins as detected by immunodetection of protein-bound DNP after derivatization with hydrazine.
Mentions: 1D-PAGE analysis of total protein extracts confirmed the reduction of cruciferin and napin proteins in dry seeds of the crua crub cruc and RNAi-napin mutant, respectively (Fig. 6A). Carbonylation of seed proteins was significant in both AR and aged seeds, with cruciferin being a major target in the wild-type and RNAi-napin lines (Fig. 6B). The cruciferin mutant exhibited a different protein carbonylation pattern in which carbonylation levels increased for the remaining proteins compared to the wild-type profile. In addition, there is a slight reduction in protein oxidation profiles comparing aged to AR seeds of all three genotypes, but also this effect was the strongest in the crua crub cruc mutant. Our result provides the first proof that SSPs, mainly cruciferins, are buffers for oxidative stress especially in dry seeds during storage. The carbonylated proteins in SSP mutants are interesting, since they will reveal new insights on the elements important for seed longevity.

Bottom Line: Proteomics approaches have been a useful tool for determining the biological roles and functions of individual proteins and identifying the molecular mechanisms that govern seed germination, vigour and viability in response to ageing.Results confirmed the role of antioxidant systems, notably vitamin E, and indicated that protection and maintenance of the translation machinery and energy pathways are essential for seed longevity.Cruciferins (CRUs) are the most abundant SSPs in Arabidopsis and seeds of a triple mutant for three CRU isoforms (crua crub cruc) were more sensitive to artificial ageing and their seed proteins were highly oxidized compared with wild-type seeds.

View Article: PubMed Central - PubMed

Affiliation: Wageningen Seed Lab, Laboratory of Plant Physiology, Wageningen University, 6708 PB Wageningen, The Netherlands Department of Molecular Plant Physiology, Utrecht University, 3584 CH Utrecht, The Netherlands.

No MeSH data available.