Table 2.
No. | Spot no. | Protein name | Accession | MWa (kDa) | pIb | Protein scorec | Seq. Cov [%]d | Reference organism | Protein function | Fold changee | |
---|---|---|---|---|---|---|---|---|---|---|---|
DH28 | DH19 | ||||||||||
Up-regulated in responsive line (DH28) and slightly changed in recalcitrant line (DH19) | |||||||||||
1 | 8609 | V-type proton ATPase catalytic subunit A | VATA_HORVU | 64.1 | 5.3 | 468.2 | 23.4 | Hordeum vulgare | Energy processes | 2.7 | 1.5 |
Down-regulated in responsive line (DH28) and slightly changed in recalcitrant line (DH19) | |||||||||||
2 | 206 | Glyceraldehyde-3-phosphate dehydrogenase 1. cytosolic | G3PC1_HORVU | 36.5 | 6.8 | 956.8 | 31.8 | Hordeum vulgare | Carbohydrate metabolism | − 2.2 | − 1.3 |
3 | 6716 | Ribose-5-phosphate isomerase A | RPIA_RHOS5 | 27.0 | 4.7 | 45.2 | 3.8 | Rhodobacter sphaeroides | Carbohydrate metabolism | − 2.0 | − 5.0 |
4 | 4302 | ATP synthase subunit beta. mitochondrial | ATPBM_ORYSJ | 58.9 | 5.9 | 282.0 | 10.9 | Oryza sativa subsp. japonica | Energy processes | − 2.0 | − 1.5 |
Two DH lines of triticale differ significantly in ME responsiveness (highly recalcitrant DH19 and responsive DH28). Swiss-Prot database was used for protein identification. The results are based on nano LC–MS/MS analyses.
aThe theoretical molecular weight (MW. kDa) and b isoelectric point (pI) retrieved from the protein database.
cThe score and dprotein sequence coverage (Score in Flex Analysis software).
eChange in abundance was calculated by dividing the mean %vol of a spot in anthers isolated form low temperature treated tillers (3 weeks at 4 °C) to mean %vol of that spot in anthers isolated from AC treated tillers (10 µM).