Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics
文献类型：期刊论文
| 作者 | Dai, Shaojun1,3; Wei, Sijia1; Bian, Yangyang4; Zhao, Qi3; Chen, Sixue2; Mao, Jiawei4; Song, Chunxia4; Cheng, Kai4; Xiao, Zhen3; Zhang, Chuanfang3 |
| 刊名 | FRONTIERS IN PLANT SCIENCE
 |
| 出版日期 | 2017-05-23 |
| 卷号 | 8 |
| 关键词 | Palmella Formation Dunaliella Salina Salinity Stress Quantitative Proteomics Phosphoproteomics |
| DOI | 10.3389/fpls.2017.00810 |
| 英文摘要 | Palmella stage is critical for some unicellular algae to survive in extreme environments. The halotolerant algae Dunaliella salina is a good single-cell model for studying plant adaptation to high salinity. To investigate the molecular adaptation mechanism in salinity shock-induced palmella formation, we performed a comprehensive physiological, proteomics and phosphoproteomics study upon palmella formation of D. salina using dimethyl labeling and Ti4+-immobilized metal ion affinity chromatography (IMAC) proteomic approaches. We found that 151 salinity-responsive proteins and 35 salinity-responsive phosphoproteins were involved in multiple signaling and metabolic pathways upon palmella formation. Taken together with photosynthetic parameters and enzyme activity analyses, the patterns of protein accumulation and phosphorylation level exhibited the mechanisms upon palmella formation, including dynamics of cytoskeleton and cell membrane curvature, accumulation and transport of exopolysaccharides, photosynthesis and energy supplying (i.e., photosystem II stability and activity, cyclic electron transport, and C4 pathway), nuclear/chloroplastic gene expression regulation and protein processing, reactive oxygen species homeostasis, and salt signaling transduction. The salinity-responsive protein-protein interaction (PPI) networks implied that signaling and protein synthesis and fate are crucial for modulation of these processes. Importantly, the 3D structure of phosphoprotein clearly indicated that the phosphorylation sites of eight proteins were localized in the region of function domain. |
| 语种 | 英语 |
| WOS记录号 | WOS:000402030500001 |
| 源URL | [http://cas-ir.dicp.ac.cn/handle/321008/152225]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 作者单位 | 1.Northeast Forestry Univ, Alkali Soil Nat Environm Sci Ctr, Key Lab Saline Alkali Vegetat Ecol Restorat Oil F, Minist Educ, Harbin, Peoples R China 2.Univ Florida, Dept Biol, Interdisciplinary Ctr Biotechnol Res, Genet Inst,Plant Mol & Cellular Biol Program, Gainesville, FL USA 3.Shanghai Normal Univ, Coll Life & Environm Sci, Shanghai, Peoples R China 4.Chinese Acad Sci, Key Lab Separat Sci Analyt Chem, Natl Chromatog R&A Ctr, Dalian Inst Chem Phys, Dalian, Peoples R China |
| 推荐引用方式 GB/T 7714 | Dai, Shaojun,Wei, Sijia,Bian, Yangyang,et al. Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics[J]. FRONTIERS IN PLANT SCIENCE,2017,8. |
| APA | Dai, Shaojun.,Wei, Sijia.,Bian, Yangyang.,Zhao, Qi.,Chen, Sixue.,...&Ye, Mingliang.(2017).Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics.FRONTIERS IN PLANT SCIENCE,8. |
| MLA | Dai, Shaojun,et al."Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics".FRONTIERS IN PLANT SCIENCE 8(2017). |
入库方式： OAI收割
来源：大连化学物理研究所
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