Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp Strain PCC 7002
文献类型：期刊论文
| 作者 | Yang, Ming-kun1; Qiao, Zhi-xian1,2; Zhang, Wan-yi1; Xiong, Qian1; Zhang, Jia1; Li, Tao1; Ge, Feng1; Zhao, Jin-dong1 |
| 刊名 | JOURNAL OF PROTEOME RESEARCH
 |
| 出版日期 | 2013-04-01 |
| 卷号 | 12期号:4页码:1909-1923 |
| 关键词 | Cyanobacteria Synechococcus sp PCC 7002 phosphoproteomics two-component signaling pathway photosynthesis |
| ISSN号 | 1535-3893 |
| 通讯作者 | Ge, F (reprint author), Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China. |
| 中文摘要 | 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. |
| 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. |
| 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 ; SIGNAL-TRANSDUCTION ; STATE TRANSITIONS ; SER/THR/TYR PHOSPHOPROTEOME ; PEPTIDE IDENTIFICATION ; INTERACTION NETWORKS ; BACTERIAL PROTEINS ; KINASES ; SYSTEMS |
| 收录类别 | SCI |
| 资助信息 | 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 |
| 语种 | 英语 |
| WOS记录号 | WOS:000317327500034 |
| 公开日期 | 2013-10-31 |
| 源URL | [http://ir.ihb.ac.cn/handle/342005/19338]  |
| 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, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100039, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Ming-kun,Qiao, Zhi-xian,Zhang, Wan-yi,et al. Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp Strain PCC 7002[J]. JOURNAL OF PROTEOME RESEARCH,2013,12(4):1909-1923. |
| APA | Yang, Ming-kun.,Qiao, Zhi-xian.,Zhang, Wan-yi.,Xiong, Qian.,Zhang, Jia.,...&Zhao, Jin-dong.(2013).Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp Strain PCC 7002.JOURNAL OF PROTEOME RESEARCH,12(4),1909-1923. |
| MLA | Yang, Ming-kun,et al."Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp Strain PCC 7002".JOURNAL OF PROTEOME RESEARCH 12.4(2013):1909-1923. |
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来源：水生生物研究所
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