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题名: Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics
作者: Wei, Sijia1;  Bian, Yangyang2;  Zhao, Qi3;  Chen, Sixue4;  Mao, Jiawei2;  Song, Chunxia2;  Cheng, Kai2;  Xiao, Zhen3;  Zhang, Chuanfang3;  Ma, Weimin3;  Zou, Hanfa2;  Ye, Mingliang2;  Dai, Shaojun1, 3
关键词: palmella formation ;  Dunaliella salina ;  salinity stress ;  quantitative proteomics ;  phosphoproteomics
刊名: FRONTIERS IN PLANT SCIENCE
发表日期: 2017-05-23
DOI: 10.3389/fpls.2017.00810
卷: 8
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Plant Sciences
研究领域[WOS]: Plant Sciences
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.
关键词[WOS]: ION AFFINITY-CHROMATOGRAPHY ;  STRESS-RESPONSIVE PROTEINS ;  CALMODULIN-BINDING PROTEIN ;  CHLAMYDOMONAS-REINHARDTII ;  SALT STRESS ;  HAEMATOCOCCUS-PLUVIALIS ;  OXIDATIVE STRESS ;  HIGH LIGHT ;  SACCHAROMYCES-CEREVISIAE ;  TRANSLATION INITIATION
语种: 英语
WOS记录号: WOS:000402030500001
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/152225
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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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.Chinese Acad Sci, Key Lab Separat Sci Analyt Chem, Natl Chromatog R&A Ctr, Dalian Inst Chem Phys, Dalian, Peoples R China
3.Shanghai Normal Univ, Coll Life & Environm Sci, Shanghai, Peoples R China
4.Univ Florida, Dept Biol, Interdisciplinary Ctr Biotechnol Res, Genet Inst,Plant Mol & Cellular Biol Program, Gainesville, FL USA

Recommended Citation:
Wei, Sijia,Bian, Yangyang,Zhao, Qi,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.
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