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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.


Related in: MedlinePlus

Principal component analysis (PCA) for proteome profiles of Ler and the near-isogenic lines NILGAAS1, NILGAAS2 and NILGAAS5. PCA was performed on the differentially accumulated protein spots in the seven comparisons (n=309).
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Figure 3: Principal component analysis (PCA) for proteome profiles of Ler and the near-isogenic lines NILGAAS1, NILGAAS2 and NILGAAS5. PCA was performed on the differentially accumulated protein spots in the seven comparisons (n=309).

Mentions: Proteomic profiling for AR and aged seeds was performed to identify mechanisms and modifications associated with the loss of germination ability during seed dry storage. Total soluble protein extracts were separated using 2D PAGE (Fig. 2A) and seven pair-wise comparisons were made (Supplementary Fig. S1). Pair-wise comparisons between the two physiological states (aged versus AR) for each genotype revealed protein spots that were affected by ageing (57 for Ler, 89 for NILGAAS1, 109 for NILGAAS2, and 126 for NILGAAS5). The three NILs contain introgression fragments at different genome positions and exhibit different levels of seed longevity. The differences in seed longevity could result from proteome variation already present in the AR seeds, which can be revealed by pair-wise comparisons between the NILs and Ler. Comparison with the AR Ler seed proteome allowed the identification of 51, 16 and 11 genotype-specific protein spots for NILGAAS1, NILGAAS2 and NILGAAS5, respectively. Some of these protein spots (8, 2 and 2, respectively) overlapped with the aged versus AR comparison (Table 1A). A total of 309 differentially accumulated protein spots were detected in the seven pair-wise comparisons (Supplementary Fig. S1). Principal component analysis (PCA) on the 309 protein spots separated the samples into two groups which represented the two physiological states (AR and aged seeds; Fig. 3). The time component (storage) accounted for 24% of the variation and the genotype component explained 11%. NILGAAS1 was the most distinct genotype, and separation of its aged seeds in the PCA might reflect its better longevity on the time component. NILGAAS5 is the least storable genotype (Fig. 3). The aged versus AR physiological state comparisons for the four genotypes showed a total of 247 protein spots whose abundance changed significantly (P≤0.05) upon ageing (Fig. 4A). A large number of the 247 spots were genotype specific (15 for Ler, 41 for NILGAAS1, 46 for NILGAAS2, and 64 for NILGAAS5) (Fig. 4A). The three genotype comparisons led to the identification of 74 altered protein spots (Fig. 4B), of which most were unique to the genotypes (47 for NILGAAS1, 12 for NILGAAS2, and 11 for NILGAAS5) (Fig. 4B). The four spots in common between NILGAAS1 and NILGAAS2 (Fig. 4B; Supplementary Table S2) when compared with Ler at the AR state might play a role in seed longevity, because both genotypes are more storable than Ler.


A role for seed storage proteins in Arabidopsis seed longevity.

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

Principal component analysis (PCA) for proteome profiles of Ler and the near-isogenic lines NILGAAS1, NILGAAS2 and NILGAAS5. PCA was performed on the differentially accumulated protein spots in the seven comparisons (n=309).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 3: Principal component analysis (PCA) for proteome profiles of Ler and the near-isogenic lines NILGAAS1, NILGAAS2 and NILGAAS5. PCA was performed on the differentially accumulated protein spots in the seven comparisons (n=309).
Mentions: Proteomic profiling for AR and aged seeds was performed to identify mechanisms and modifications associated with the loss of germination ability during seed dry storage. Total soluble protein extracts were separated using 2D PAGE (Fig. 2A) and seven pair-wise comparisons were made (Supplementary Fig. S1). Pair-wise comparisons between the two physiological states (aged versus AR) for each genotype revealed protein spots that were affected by ageing (57 for Ler, 89 for NILGAAS1, 109 for NILGAAS2, and 126 for NILGAAS5). The three NILs contain introgression fragments at different genome positions and exhibit different levels of seed longevity. The differences in seed longevity could result from proteome variation already present in the AR seeds, which can be revealed by pair-wise comparisons between the NILs and Ler. Comparison with the AR Ler seed proteome allowed the identification of 51, 16 and 11 genotype-specific protein spots for NILGAAS1, NILGAAS2 and NILGAAS5, respectively. Some of these protein spots (8, 2 and 2, respectively) overlapped with the aged versus AR comparison (Table 1A). A total of 309 differentially accumulated protein spots were detected in the seven pair-wise comparisons (Supplementary Fig. S1). Principal component analysis (PCA) on the 309 protein spots separated the samples into two groups which represented the two physiological states (AR and aged seeds; Fig. 3). The time component (storage) accounted for 24% of the variation and the genotype component explained 11%. NILGAAS1 was the most distinct genotype, and separation of its aged seeds in the PCA might reflect its better longevity on the time component. NILGAAS5 is the least storable genotype (Fig. 3). The aged versus AR physiological state comparisons for the four genotypes showed a total of 247 protein spots whose abundance changed significantly (P≤0.05) upon ageing (Fig. 4A). A large number of the 247 spots were genotype specific (15 for Ler, 41 for NILGAAS1, 46 for NILGAAS2, and 64 for NILGAAS5) (Fig. 4A). The three genotype comparisons led to the identification of 74 altered protein spots (Fig. 4B), of which most were unique to the genotypes (47 for NILGAAS1, 12 for NILGAAS2, and 11 for NILGAAS5) (Fig. 4B). The four spots in common between NILGAAS1 and NILGAAS2 (Fig. 4B; Supplementary Table S2) when compared with Ler at the AR state might play a role in seed longevity, because both genotypes are more storable than Ler.

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.


Related in: MedlinePlus