Table I.
Arabidopsis proteins whose abundance significantly increased in dry mature seeds according to controlled deterioration time
AGI, Arabidopsis Genome Initiative.
No.a | Experimental Molecular Mass | Experimental pI | Arabidopsis Protein Name | Theoretical Molecular Mass | Theoretical pI | AGI No. | Coverage | Relative Abundanceb | T1/2 |
---|---|---|---|---|---|---|---|---|---|
kD | kD | ratio 7 d:0 d | d | ||||||
7c | 37.55 | 5.09 | 60S acidic ribosomal protein | 34.37 | 5.08 | At3g11250 | 24% | 3.4 ± 0.1 | 2.2 ± 0.3 |
212d | 42.57 | 5.18 | Actin 2 | 41.21 | 5.43 | At3g18780 | 33% | 2.5 ± 0.4 | 5.2 ± 2.7 |
253d | 40.29 | 5.84 | Glyceraldehyde-3-P dehydrogenase, cytosolic | 36.99 | 6.34 | At3g04120 | 18% | >16 | >7 |
293d | 96.69 | 5.61 | Peptidase M1 family protein | 103.40 | 6.09 | At1g63770 | 4% | >5.1 | >7 |
302d | 40.34 | 6.03 | Glyceraldehyde-3-P dehydrogenase | 36.90 | 7.21 | At1g13440 | 30% | 7.7 ± 1.4 | 6.1 ± 2.0 |
305d | 68.25 | 5.70 | Phosphoglucomutase | 63.46 | 5.57 | At1g70730 | 34% | 2.2 ± 0.1 | 1.3 ± 0.4 |
308c | 28.52 | 5.89 | α-Cruciferin 12S (seed storage protein fragment) | 50.56 | 6.53 | At1g03880 | 10% | 3.4 ± 0.5 | 4.8 ± 1.7 |
312c | 14.21 | 3.82 | NADP-dependent glyceraldehyde-3-P dehydrogenase (fragment) | 53.04 | 6.61 | At2g24270 | 8% | 6.0 ± 0.3 | 1.8 ± 0.3 |
320c | 57.36 | 5.82 | Ribulose bisphosphate carboxylase large chain | 53.47 | 6.25 | AtCg00490 | 24% | >2.7 | >7 |
321c | 57.36 | 5.84 | Ribulose bisphosphate carboxylase large chain | 53.47 | 6.25 | AtCg00490 | 28% | >2.8 | >7 |
322c | 35.21 | 5.20 | 60S acidic ribosomal protein | 33.65 | 4.93 | At2g40010 | 15% | >4.4 | >7 |
376d | 57.35 | 4.92 | Tubulin β-8 chain | 50.59 | 4.46 | At5g23860 | 9% | 5.0 ± 0.2 | 1.5 ± 0.2 |
Protein numbering following Arabidopsis seed protein reference maps available at http://www.seed-proteome.com.
Data obtained from densitometric analysis of individual spots from proteins on 2D gels stained with silver nitrate (see Fig. 2A for an example of a 2D gel): normalized spot volume in the deteriorated seeds (7 d of CDT) divided by the normalized spot volume in the nondeteriorated control seeds (0 d of CDT), from five different gels and three independent extractions.
Listed proteins correspond to previously identified proteins (Gallardo et al., 2001, 2002a; Rajjou et al., 2004, 2006a; Job et al., 2005).
Listed proteins correspond to proteins identified during this work; the peptide sequences determined are available in Supplemental Table S2.