中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Phosphoproteomic Analysis Provides Novel Insights into Stress Responses in Phaeodactylum tricornutum, a Model Diatom

文献类型:期刊论文

作者Chen, Zhuo1; Yang, Ming-kun2; Li, Chong-yang2; Wang, Yan2; Zhang, Jia2; Wang, Dian-bing3; Zhang, Xian-en1,3; Ge, Feng2
刊名JOURNAL OF PROTEOME RESEARCH
出版日期2014-05-01
卷号13期号:5页码:2511-2523
关键词diatom Phaeodactylum tricornutum phosphoproteomics stress responses
ISSN号1535-3893
通讯作者Zhang, XE (reprint author), Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China.
中文摘要Protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) is well established as a key regulatory posttranslational modification used in signal transduction to control cell growth, proliferation, and stress responses. However, little is known about its extent and function in diatoms. Phaeodactylum tricornutum is a unicellular marine diatom that has been used as a model organism for research on diatom molecular biology. Although more than 1000 protein kinases and phosphatases with specificity for Ser/Thr/Tyr residues have been predicted in P. tricornutum, no phosphorylation event has so far been revealed by classical biochemical approaches. Here, we performed a global phosphoproteomic analysis combining protein/peptide fractionation, TiO2 enrichment, and LC-MS/MS analyses. In total, we identified 264 unique phosphopeptides, including 434 in vivo phosphorylated sites on 245 phosphoproteins. The phosphorylated proteins were implicated in the regulation of diverse biological processes, including signaling, metabolic pathways, and stress responses. Six identified phosphoproteins were further validated by Western blotting using phospho-specific antibodies. The functions of these proteins are discussed in the context of signal transduction networks in P. tricornutum. Our results advance the current understanding of diatom biology and will be useful for elucidating the phosphor-relay signaling networks in this model diatom.
英文摘要Protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) is well established as a key regulatory posttranslational modification used in signal transduction to control cell growth, proliferation, and stress responses. However, little is known about its extent and function in diatoms. Phaeodactylum tricornutum is a unicellular marine diatom that has been used as a model organism for research on diatom molecular biology. Although more than 1000 protein kinases and phosphatases with specificity for Ser/Thr/Tyr residues have been predicted in P. tricornutum, no phosphorylation event has so far been revealed by classical biochemical approaches. Here, we performed a global phosphoproteomic analysis combining protein/peptide fractionation, TiO2 enrichment, and LC-MS/MS analyses. In total, we identified 264 unique phosphopeptides, including 434 in vivo phosphorylated sites on 245 phosphoproteins. The phosphorylated proteins were implicated in the regulation of diverse biological processes, including signaling, metabolic pathways, and stress responses. Six identified phosphoproteins were further validated by Western blotting using phospho-specific antibodies. The functions of these proteins are discussed in the context of signal transduction networks in P. tricornutum. Our results advance the current understanding of diatom biology and will be useful for elucidating the phosphor-relay signaling networks in this model diatom.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemical Research Methods
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]TANDEM MASS-SPECTROMETRY ; PROTEIN-PHOSPHORYLATION MOTIFS ; MARINE DIATOM ; THALASSIOSIRA-PSEUDONANA ; CHLAMYDOMONAS-REINHARDTII ; LIPID-ACCUMULATION ; NITRIC-OXIDE ; PEPTIDE IDENTIFICATION ; PROTEOMIC ANALYSIS ; IN-VIVO
收录类别SCI
资助信息National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program
语种英语
WOS记录号WOS:000335490600024
公开日期2014-08-13
源URL[http://ir.ihb.ac.cn/handle/342005/20085]  
专题水生生物研究所_水生生物分子与细胞生物学研究中心_期刊论文
作者单位1.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
3.Chinese Acad Sci, Inst Biophys, State Key Lab Biomacromol, Beijing 100080, Peoples R China
推荐引用方式
GB/T 7714
Chen, Zhuo,Yang, Ming-kun,Li, Chong-yang,et al. Phosphoproteomic Analysis Provides Novel Insights into Stress Responses in Phaeodactylum tricornutum, a Model Diatom[J]. JOURNAL OF PROTEOME RESEARCH,2014,13(5):2511-2523.
APA Chen, Zhuo.,Yang, Ming-kun.,Li, Chong-yang.,Wang, Yan.,Zhang, Jia.,...&Ge, Feng.(2014).Phosphoproteomic Analysis Provides Novel Insights into Stress Responses in Phaeodactylum tricornutum, a Model Diatom.JOURNAL OF PROTEOME RESEARCH,13(5),2511-2523.
MLA Chen, Zhuo,et al."Phosphoproteomic Analysis Provides Novel Insights into Stress Responses in Phaeodactylum tricornutum, a Model Diatom".JOURNAL OF PROTEOME RESEARCH 13.5(2014):2511-2523.

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来源:水生生物研究所

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