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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

(A) Principle component analysis (PCA): red circles show the position of salt stress spot maps and blue drought stress spot maps and green circles are the controls; numbers indicate the corresponding sample numbers. (B) Photo of raw protein extracts before solubilization: in the upper row are the controls, in the middle one salt stress samples, and in the lower row the drought stress samples, all of them in chronological order from left to right.
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fig2: (A) Principle component analysis (PCA): red circles show the position of salt stress spot maps and blue drought stress spot maps and green circles are the controls; numbers indicate the corresponding sample numbers. (B) Photo of raw protein extracts before solubilization: in the upper row are the controls, in the middle one salt stress samples, and in the lower row the drought stress samples, all of them in chronological order from left to right.

Mentions: For DIGE analysis, spots were detected on all scans and intergel matching was performed using the DeCyder software. The matching was manually checked and corrected in mismatched regions. In the next step, a PCA analysis was performed. PCA helps to identify some underlying sources of variation and gives first impression on how well experimental groups can be separated. Spots that could be localized on 80% of spot maps (gel scans) were included in the analysis (Figure 2).


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)

(A) Principle component analysis (PCA): red circles show the position of salt stress spot maps and blue drought stress spot maps and green circles are the controls; numbers indicate the corresponding sample numbers. (B) Photo of raw protein extracts before solubilization: in the upper row are the controls, in the middle one salt stress samples, and in the lower row the drought stress samples, all of them in chronological order from left to right.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig2: (A) Principle component analysis (PCA): red circles show the position of salt stress spot maps and blue drought stress spot maps and green circles are the controls; numbers indicate the corresponding sample numbers. (B) Photo of raw protein extracts before solubilization: in the upper row are the controls, in the middle one salt stress samples, and in the lower row the drought stress samples, all of them in chronological order from left to right.
Mentions: For DIGE analysis, spots were detected on all scans and intergel matching was performed using the DeCyder software. The matching was manually checked and corrected in mismatched regions. In the next step, a PCA analysis was performed. PCA helps to identify some underlying sources of variation and gives first impression on how well experimental groups can be separated. Spots that could be localized on 80% of spot maps (gel scans) were included in the analysis (Figure 2).

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