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题名: Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp Strain PCC 7002
作者: Yang, Ming-kun1; Qiao, Zhi-xian1, 2; Zhang, Wan-yi1; Xiong, Qian1; Zhang, Jia1; Li, Tao1; Ge, Feng1; Zhao, Jin-dong1
通讯作者: Ge, F (reprint author), Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China.
关键词: Cyanobacteria ; Synechococcus sp PCC 7002 ; phosphoproteomics ; two-component signaling pathway ; photosynthesis
刊名: JOURNAL OF PROTEOME RESEARCH
发表日期: 2013-04-01
DOI: 10.1021/pr4000043
卷: 12, 期:4, 页:1909-1923
收录类别: SCI
文章类型: Article
部门归属: [Yang, Ming-kun; Qiao, Zhi-xian; Zhang, Wan-yi; Xiong, Qian; Zhang, Jia; Li, Tao; Ge, Feng; Zhao, Jin-dong] Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China; [Qiao, Zhi-xian] Univ Chinese Acad Sci, Beijing 100039, Peoples R China
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
资助者: National Basic Research Program of China (973 Program) [2012CB518700]; National Natural Science Foundation of China [31000113]; Hundred Talents Program of the Chinese Academy of Sciences
类目[WOS]: Biochemical Research Methods
研究领域[WOS]: Biochemistry & Molecular Biology
摘要: Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr), and tyrosine (Tyr) residues is one of the major post-translational modifications in the bacteria, involved in regulating a myriad of physiological processes. Cyanobacteria are one of the largest groups of bacteria and are the only prokaryotes capable of oxygenic photosynthesis. Many cyanobacteria strains contain unusually high numbers of protein kinases and phosphatases with specificity on Ser, Thr, and Tyr residues. However, only a few dozen phosphorylation sites in cyanobacteria are known, presenting a major obstacle for further understanding the regulatory roles of reversible phosphorylation in this group of bacteria. In this study, we carried out a global and site-specific phosphoproteomic analysis on the model cyanobacterium Synechococcus sp. PCC 7002. In total, 280 phosphopeptides and 410 phosphorylation sites from 245 Synechococcus sp. PCC 7002 proteins were identified through the combined use of protein/peptide prefractionation, TiO2 enrichment, and LC-MS/MS analysis. The identified phosphoproteins were functionally categorized into an interaction map and found to be involved in various biological processes such as two-component signaling pathway and photosynthesis. Our data provide the first global survey of phosphorylation in cyanobacteria by using a phosphoproteomic approach and suggest a wide-ranging regulatory scope of this modification. The provided data set may help reveal the physiological functions underlying Ser/Thr/Tyr phosphorylation and facilitate the elucidation of the entire signaling networks in cyanobacteria.
英文摘要: Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr), and tyrosine (Tyr) residues is one of the major post-translational modifications in the bacteria, involved in regulating a myriad of physiological processes. Cyanobacteria are one of the largest groups of bacteria and are the only prokaryotes capable of oxygenic photosynthesis. Many cyanobacteria strains contain unusually high numbers of protein kinases and phosphatases with specificity on Ser, Thr, and Tyr residues. However, only a few dozen phosphorylation sites in cyanobacteria are known, presenting a major obstacle for further understanding the regulatory roles of reversible phosphorylation in this group of bacteria. In this study, we carried out a global and site-specific phosphoproteomic analysis on the model cyanobacterium Synechococcus sp. PCC 7002. In total, 280 phosphopeptides and 410 phosphorylation sites from 245 Synechococcus sp. PCC 7002 proteins were identified through the combined use of protein/peptide prefractionation, TiO2 enrichment, and LC-MS/MS analysis. The identified phosphoproteins were functionally categorized into an interaction map and found to be involved in various biological processes such as two-component signaling pathway and photosynthesis. Our data provide the first global survey of phosphorylation in cyanobacteria by using a phosphoproteomic approach and suggest a wide-ranging regulatory scope of this modification. The provided data set may help reveal the physiological functions underlying Ser/Thr/Tyr phosphorylation and facilitate the elucidation of the entire signaling networks in cyanobacteria.
关键词[WOS]: TANDEM MASS-SPECTROMETRY ; PROTEIN-PHOSPHORYLATION ; SIGNAL-TRANSDUCTION ; STATE TRANSITIONS ; SER/THR/TYR PHOSPHOPROTEOME ; PEPTIDE IDENTIFICATION ; INTERACTION NETWORKS ; BACTERIAL PROTEINS ; KINASES ; SYSTEMS
语种: 英语
WOS记录号: WOS:000317327500034
ISSN号: 1535-3893
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/342005/19338
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 Algal Biol, Wuhan 430072, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100039, Peoples R China
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