| Phosphoproteomic Analysis Provides Novel Insights into Stress Responses in Phaeodactylum tricornutum, a Model Diatom | |
| Chen, Zhuo1; Yang, Ming-kun2; Li, Chong-yang2; Wang, Yan2; Zhang, Jia2; Wang, Dian-bing3; Zhang, Xian-en1,3; Ge, Feng2; Zhang, XE (reprint author), Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China. | |
| 2014-05-01 | |
| Source Publication | JOURNAL OF PROTEOME RESEARCH
 |
| ISSN | 1535-3893 |
| Volume | 13Issue:5Pages:2511-2523 |
| Abstract | 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.; 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. |
| Subtype | Article |
| Keyword | Diatom Phaeodactylum Tricornutum Phosphoproteomics Stress Responses |
| Department | [Chen, Zhuo; Zhang, Xian-en] Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China; [Yang, Ming-kun; Li, Chong-yang; Wang, Yan; Zhang, Jia; Ge, Feng] Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China; [Wang, Dian-bing; Zhang, Xian-en] Chinese Acad Sci, Inst Biophys, State Key Lab Biomacromol, Beijing 100080, Peoples R China |
| DOI | 10.1021/pr401290u |
| WOS Headings | Science & Technology ; Life Sciences & Biomedicine |
| Funding Organization | National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program ; National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program ; National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program ; National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program |
| Indexed By | SCI |
| Language | 英语 |
| WOS Research Area | Biochemistry & Molecular Biology |
| WOS Subject | Biochemical Research Methods |
| WOS ID | WOS:000335490600024 |
| WOS Keyword | TANDEM MASS-SPECTROMETRY ; PROTEIN-PHOSPHORYLATION MOTIFS ; MARINE DIATOM ; THALASSIOSIRA-PSEUDONANA ; CHLAMYDOMONAS-REINHARDTII ; LIPID-ACCUMULATION ; NITRIC-OXIDE ; PEPTIDE IDENTIFICATION ; PROTEOMIC ANALYSIS ; IN-VIVO |
| Funding Organization | National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program ; National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program ; National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program ; National Natural Science Foundation of China [31370746]; Hundred Talents Program of the Chinese Academy of Sciences; State Key Laboratory Program |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.ihb.ac.cn/handle/342005/20085 |
| Collection | 水生生物分子与细胞生物学研究中心_期刊论文 |
| Corresponding Author | Zhang, XE (reprint author), Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China. |
| Affiliation | 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 |
| Recommended Citation 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.,...&Zhang, XE .(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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