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Proteome Analysis for Understanding Abiotic Stress (Salinity and Drought) Tolerance in Date Palm (Phoenix dactylifera L.).

El Rabey HA, Al-Malki AL, Abulnaja KO, Rohde W - Int J Genomics (2015)

Bottom Line: Mass spectrometric analysis identified 12 proteins; three out of them were significantly changed under both salt and drought stress, while the other nine were significantly changed only in salt-stressed plants.The levels of ATP synthase alpha and beta subunits, an unknown protein and some of RubisCO fragments were significantly changed under both salt and drought stress conditions.Changes in abundance of superoxide dismutase, chlorophyll A-B binding protein, light-harvesting complex1 protein Lhca1, RubisCO activase, phosphoglycerate kinase, chloroplast light-harvesting chlorophyll a/b-binding protein, phosphoribulokinase, transketolase, RubisCO, and some of RubisCO fragments were significant only for salt stress.

View Article: PubMed Central - PubMed

Affiliation: Biochemistry Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia ; Bioinformatics Department, Genetic Engineering and Biotechnology Institute, Sadat City University, Sadat City, Minufiya, Egypt.

ABSTRACT
This study was carried out to study the proteome of date palm under salinity and drought stress conditions to possibly identify proteins involved in stress tolerance. For this purpose, three-month-old seedlings of date palm cultivar "Sagie" were subjected to drought (27.5 g/L polyethylene glycol 6000) and salinity stress conditions (16 g/L NaCl) for one month. DIGE analysis of protein extracts identified 47 differentially expressed proteins in leaves of salt- and drought-treated palm seedlings. Mass spectrometric analysis identified 12 proteins; three out of them were significantly changed under both salt and drought stress, while the other nine were significantly changed only in salt-stressed plants. The levels of ATP synthase alpha and beta subunits, an unknown protein and some of RubisCO fragments were significantly changed under both salt and drought stress conditions. Changes in abundance of superoxide dismutase, chlorophyll A-B binding protein, light-harvesting complex1 protein Lhca1, RubisCO activase, phosphoglycerate kinase, chloroplast light-harvesting chlorophyll a/b-binding protein, phosphoribulokinase, transketolase, RubisCO, and some of RubisCO fragments were significant only for salt stress.

No MeSH data available.


Related in: MedlinePlus

The identified proteins shown on the scan of preparative gel. Proteins in the spots marked with the red circle could not be identified. The color code used in protein name boxes is the same as in Table 3.
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fig7: The identified proteins shown on the scan of preparative gel. Proteins in the spots marked with the red circle could not be identified. The color code used in protein name boxes is the same as in Table 3.

Mentions: Forty-seven spots were cut from the preparative gel for MS analysis. Proteins in the gel plugs were reduced with 10 mM dithiothreitol and alkylated using 55 mM iodoacetamide in 0.1 M to open S-S bridges for action of trypsin. Digestion with trypsin (12.5 ng/μL of trypsin in 50 mM NH4HCO3) was performed overnight at 37°C. The resulting peptides were extracted from the gel plugs in two extraction steps: first one with 25 mM NH4HCO3 and second one with 5% formic acid. Collected extracts were dried down and resolubilized in 2% acetonitrile with 0.1% formic acid in water (MS grade) for MS analysis. The resulting peptides were separated according to their hydrophobicity by nano-HPLC (C18 column, UltiMate 3000 HPLC system, Dionex) and sprayed directly into an ion trap spectrometer (amaZon ETD, Bruker Daltonics) using nano-ESI sprayer. Processed MS/MS spectra were used for the protein identification with in-house Mascot Search server (Matrix Science software). Swiss Prot (All species) and NCBInr (Green plants) databases were involved in the protein search (Figure 7 and Table 3).


Proteome Analysis for Understanding Abiotic Stress (Salinity and Drought) Tolerance in Date Palm (Phoenix dactylifera L.).

El Rabey HA, Al-Malki AL, Abulnaja KO, Rohde W - Int J Genomics (2015)

The identified proteins shown on the scan of preparative gel. Proteins in the spots marked with the red circle could not be identified. The color code used in protein name boxes is the same as in Table 3.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4488584&req=5

fig7: The identified proteins shown on the scan of preparative gel. Proteins in the spots marked with the red circle could not be identified. The color code used in protein name boxes is the same as in Table 3.
Mentions: Forty-seven spots were cut from the preparative gel for MS analysis. Proteins in the gel plugs were reduced with 10 mM dithiothreitol and alkylated using 55 mM iodoacetamide in 0.1 M to open S-S bridges for action of trypsin. Digestion with trypsin (12.5 ng/μL of trypsin in 50 mM NH4HCO3) was performed overnight at 37°C. The resulting peptides were extracted from the gel plugs in two extraction steps: first one with 25 mM NH4HCO3 and second one with 5% formic acid. Collected extracts were dried down and resolubilized in 2% acetonitrile with 0.1% formic acid in water (MS grade) for MS analysis. The resulting peptides were separated according to their hydrophobicity by nano-HPLC (C18 column, UltiMate 3000 HPLC system, Dionex) and sprayed directly into an ion trap spectrometer (amaZon ETD, Bruker Daltonics) using nano-ESI sprayer. Processed MS/MS spectra were used for the protein identification with in-house Mascot Search server (Matrix Science software). Swiss Prot (All species) and NCBInr (Green plants) databases were involved in the protein search (Figure 7 and Table 3).

Bottom Line: Mass spectrometric analysis identified 12 proteins; three out of them were significantly changed under both salt and drought stress, while the other nine were significantly changed only in salt-stressed plants.The levels of ATP synthase alpha and beta subunits, an unknown protein and some of RubisCO fragments were significantly changed under both salt and drought stress conditions.Changes in abundance of superoxide dismutase, chlorophyll A-B binding protein, light-harvesting complex1 protein Lhca1, RubisCO activase, phosphoglycerate kinase, chloroplast light-harvesting chlorophyll a/b-binding protein, phosphoribulokinase, transketolase, RubisCO, and some of RubisCO fragments were significant only for salt stress.

View Article: PubMed Central - PubMed

Affiliation: Biochemistry Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia ; Bioinformatics Department, Genetic Engineering and Biotechnology Institute, Sadat City University, Sadat City, Minufiya, Egypt.

ABSTRACT
This study was carried out to study the proteome of date palm under salinity and drought stress conditions to possibly identify proteins involved in stress tolerance. For this purpose, three-month-old seedlings of date palm cultivar "Sagie" were subjected to drought (27.5 g/L polyethylene glycol 6000) and salinity stress conditions (16 g/L NaCl) for one month. DIGE analysis of protein extracts identified 47 differentially expressed proteins in leaves of salt- and drought-treated palm seedlings. Mass spectrometric analysis identified 12 proteins; three out of them were significantly changed under both salt and drought stress, while the other nine were significantly changed only in salt-stressed plants. The levels of ATP synthase alpha and beta subunits, an unknown protein and some of RubisCO fragments were significantly changed under both salt and drought stress conditions. Changes in abundance of superoxide dismutase, chlorophyll A-B binding protein, light-harvesting complex1 protein Lhca1, RubisCO activase, phosphoglycerate kinase, chloroplast light-harvesting chlorophyll a/b-binding protein, phosphoribulokinase, transketolase, RubisCO, and some of RubisCO fragments were significant only for salt stress.

No MeSH data available.


Related in: MedlinePlus