The beta subunit of glyceraldehyde 3-phosphate dehydrogenase is an important factor for maintaining photosynthesis and plant development under salt stress—Based on an integrative analysis of the structural, physiological and proteomic changes in chloroplasts in Thellungiella halophila. (July 2015)
- Record Type:
- Journal Article
- Title:
- The beta subunit of glyceraldehyde 3-phosphate dehydrogenase is an important factor for maintaining photosynthesis and plant development under salt stress—Based on an integrative analysis of the structural, physiological and proteomic changes in chloroplasts in Thellungiella halophila. (July 2015)
- Main Title:
- The beta subunit of glyceraldehyde 3-phosphate dehydrogenase is an important factor for maintaining photosynthesis and plant development under salt stress—Based on an integrative analysis of the structural, physiological and proteomic changes in chloroplasts in Thellungiella halophila
- Authors:
- Chang, Lili
Guo, Anping
Jin, Xiang
Yang, Qian
Wang, Dan
Sun, Yong
Huang, Qixing
Wang, Limin
Peng, Cunzhi
Wang, Xuchu - Abstract:
- Graphical abstract: Highlights: Proteomics of Thellungiella chloroplasts under salinity were firstly reported. We identified 75 salt responsive proteins from Thellungiella chloroplasts. Proteins involved in photosynthesis and energy metabolism are induced by salinity. Glyceraldehyde 3-phosphate dehydrogenase is important for plant salt tolerance. ThGAPB improve salt tolerance by keeping photosynthesis and plant development. Abstract: Thellungiella halophila, a new model halophyte, can survive under highly saline conditions. We performed comparative proteomics of chloroplasts from plants grown under different saline conditions. Seventy-five salt-responsive proteins were positively identified by mass spectrometry, which represented 43 unique ones. These proteins were categorized into 7 main pathways: light reaction, carbon fixation, energy metabolism, antenna proteins, cell structure, and protein degradation and folding. Saline conditions increased the abundance of proteins involved in photosynthesis, energy metabolism and cell structure. The results indicated that Thellungiella could withstand high salinity by maintaining normal or high photosynthetic capacity, reducing ROS production, as well as enhancing energy usage. Meanwhile, the ultrastructural and physiological data also agree with chloroplast proteomics results. Subsequently, the glyceraldehydes 3-phosphate dehydrogenase beta subunit (GAPB) involved in carbon fixation was selected and its role in salt tolerance wasGraphical abstract: Highlights: Proteomics of Thellungiella chloroplasts under salinity were firstly reported. We identified 75 salt responsive proteins from Thellungiella chloroplasts. Proteins involved in photosynthesis and energy metabolism are induced by salinity. Glyceraldehyde 3-phosphate dehydrogenase is important for plant salt tolerance. ThGAPB improve salt tolerance by keeping photosynthesis and plant development. Abstract: Thellungiella halophila, a new model halophyte, can survive under highly saline conditions. We performed comparative proteomics of chloroplasts from plants grown under different saline conditions. Seventy-five salt-responsive proteins were positively identified by mass spectrometry, which represented 43 unique ones. These proteins were categorized into 7 main pathways: light reaction, carbon fixation, energy metabolism, antenna proteins, cell structure, and protein degradation and folding. Saline conditions increased the abundance of proteins involved in photosynthesis, energy metabolism and cell structure. The results indicated that Thellungiella could withstand high salinity by maintaining normal or high photosynthetic capacity, reducing ROS production, as well as enhancing energy usage. Meanwhile, the ultrastructural and physiological data also agree with chloroplast proteomics results. Subsequently, the glyceraldehydes 3-phosphate dehydrogenase beta subunit (GAPB) involved in carbon fixation was selected and its role in salt tolerance was clarified by over-expressing it in Arabidopsis. ThGAPB-overexpressing plants had higher total chlorophyll contents, dry weights, water contents and survival rates than that of wild type plants. These results indicated that ThGAPB might improve plant salt tolerance by maintaining higher recycling rates of ADP and NADP + to decrease ROS production, helping to maintain photosynthetic efficiency and plant development under saline conditions. … (more)
- Is Part Of:
- Plant science. Volume 236(2015:Jul.)
- Journal:
- Plant science
- Issue:
- Volume 236(2015:Jul.)
- Issue Display:
- Volume 236 (2015)
- Year:
- 2015
- Volume:
- 236
- Issue Sort Value:
- 2015-0236-0000-0000
- Page Start:
- 223
- Page End:
- 238
- Publication Date:
- 2015-07
- Subjects:
- Chloroplast -- Comparative proteomics -- Glyceraldehyde 3-phosphate dehydrogenase -- Halophyte -- Thellungiella halophila
3-PGA glycerate-3-phosphate -- ATPB ATP binding -- ATPM ATP metabolic process -- CA carbonic anhydrase -- CBP chlorophyll a–b binding protein -- CU carbon utilization -- CP chloroplast protein -- Cytb559 cytochrome b559 -- FBA fructose-bisphosphate aldolase -- FNR ferredoxin-NADP reductase -- G3P glyceraldehyde 3-phosphate -- GAPB glyceraldehyde 3-phosphate dehydrogenase beta subunit -- GMP glucose metabolic process -- GPD glyceraldehyde 3-phosphate dehydrogenase -- IS internal standard -- OEC oxygen-evolving complex -- OEE oxygen-evolving enhancer protein -- ORP oxidation-reduction process -- PCL protein-chromophore linkage -- PET photosynthetic electron transport -- PLAP plastid-lipid-associated protein -- PRK phosphoribulokinase -- RCA RuBisCO activase -- SOTA self-organizing tree algorithm -- SMA structural molecule activity -- WT wild type
Botany -- Periodicals
Botanique -- Périodiques
580 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01689452 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.plantsci.2015.04.010 ↗
- Languages:
- English
- ISSNs:
- 0168-9452
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6523.390000
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British Library HMNTS - ELD Digital store - Ingest File:
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