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题名: Phosphoproteomic Analysis of Protein Phosphorylation Networks in Tetrahymena thermophila, a Model Single-celled Organism
作者: Tian, Miao1, 2; Chen, Xiulan3; Xiong, Qian1; Xiong, Jie1; Xiao, Chuanle4; Ge, Feng1; Yang, Fuquan3; Miao, Wei1
通讯作者: Tian, M (reprint author), Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Hubei, Peoples R China.
关键词: GENOME DATABASE TGD ; HUMAN LIVER-TISSUE ; MASS-SPECTROMETRY ; SACCHAROMYCES-CEREVISIAE ; MOUSE-LIVER ; IN-VIVO ; BIOLOGICAL NETWORKS ; GENE-EXPRESSION ; WIDE PREDICTION ; GLOBAL ANALYSIS
刊名: MOLECULAR & CELLULAR PROTEOMICS
发表日期: 2014-02-01
DOI: 10.1074/mcp.M112.026575
卷: 13, 期:2, 页:503-519
收录类别: SCI
文章类型: Article
部门归属: [Tian, Miao; Xiong, Qian; Xiong, Jie; Ge, Feng; Miao, Wei] Chinese Acad Sci, Inst Hydrobiol, Key Lab Aquat Biodivers & Conservat, Wuhan 430072, Hubei, Peoples R China; [Tian, Miao] Univ Chinese Acad Sci, Beijing 100049, Peoples R China; [Chen, Xiulan; Yang, Fuquan] Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China; [Xiao, Chuanle] Jinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R China
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
资助者: Projects of International Cooperation and Exchanges Ministry of Science and Technology of China [2013DFG32390]; National Natural Science Foundation of China [91231118]; Knowledge Innovation Program of CAS [KSCX2-EW-G-6-4]; Hundred Talents Program of the Chinese Academy of Sciences; National Basic Research Program of China (973) [2010CB833703, 2012CB966803]
类目[WOS]: Biochemical Research Methods
研究领域[WOS]: Biochemistry & Molecular Biology
摘要: Tetrahymena thermophila is a widely used unicellular eukaryotic model organism in biological research and contains more than 1000 protein kinases and phosphatases with specificity for Ser/Thr/Tyr residues. However, only a few dozen phosphorylation sites in T. thermophila are known, presenting a major obstacle to further understanding of the regulatory roles of reversible phosphorylation in this organism. In this study, we used high-accuracy mass-spectrometry-based proteomics to conduct global and site-specific phosphoproteome profiling of T. thermophila. In total, 1384 phosphopeptides and 2238 phosphorylation sites from 1008 T. thermophila proteins were identified through the combined use of peptide prefractionation, TiO2 enrichment, and two-dimensional LC-MS/MS analysis. The identified phosphoproteins are implicated in the regulation of various biological processes such as transport, gene expression, and mRNA metabolic process. Moreover, integrated analysis of the T. thermophila phosphoproteome and gene network revealed the potential biological functions of many previously unannotated proteins and predicted some putative kinase-substrate pairs. Our data provide the first global survey of phosphorylation in T. thermophila using a phosphoproteomic approach and suggest a wide-ranging regulatory scope of this modification. The provided dataset is a valuable resource for the future understanding of signaling pathways in this important model organism.
英文摘要: Tetrahymena thermophila is a widely used unicellular eukaryotic model organism in biological research and contains more than 1000 protein kinases and phosphatases with specificity for Ser/Thr/Tyr residues. However, only a few dozen phosphorylation sites in T. thermophila are known, presenting a major obstacle to further understanding of the regulatory roles of reversible phosphorylation in this organism. In this study, we used high-accuracy mass-spectrometry-based proteomics to conduct global and site-specific phosphoproteome profiling of T. thermophila. In total, 1384 phosphopeptides and 2238 phosphorylation sites from 1008 T. thermophila proteins were identified through the combined use of peptide prefractionation, TiO2 enrichment, and two-dimensional LC-MS/MS analysis. The identified phosphoproteins are implicated in the regulation of various biological processes such as transport, gene expression, and mRNA metabolic process. Moreover, integrated analysis of the T. thermophila phosphoproteome and gene network revealed the potential biological functions of many previously unannotated proteins and predicted some putative kinase-substrate pairs. Our data provide the first global survey of phosphorylation in T. thermophila using a phosphoproteomic approach and suggest a wide-ranging regulatory scope of this modification. The provided dataset is a valuable resource for the future understanding of signaling pathways in this important model organism.
关键词[WOS]: GENOME DATABASE TGD ; HUMAN LIVER-TISSUE ; MASS-SPECTROMETRY ; SACCHAROMYCES-CEREVISIAE ; MOUSE-LIVER ; IN-VIVO ; BIOLOGICAL NETWORKS ; GENE-EXPRESSION ; WIDE PREDICTION ; GLOBAL ANALYSIS
语种: 英语
WOS记录号: WOS:000331369000010
ISSN号: 1535-9476
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/342005/20095
Appears in Collections:水生生物分子与细胞生物学研究中心_期刊论文

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作者单位: 1.Chinese Acad Sci, Inst Hydrobiol, Key Lab Aquat Biodivers & Conservat, Wuhan 430072, Hubei, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
4.Jinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R China

Recommended Citation:
Tian, Miao; Chen, Xiulan; Xiong, Qian; Xiong, Jie; Xiao, Chuanle; Ge, Feng; Yang, Fuquan; Miao, Wei.Phosphoproteomic Analysis of Protein Phosphorylation Networks in Tetrahymena thermophila, a Model Single-celled Organism,MOLECULAR & CELLULAR PROTEOMICS,2014,13(2):503-519
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