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Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp Strain PCC 7002
Yang, Ming-kun1; Qiao, Zhi-xian1,2; Zhang, Wan-yi1; Xiong, Qian1; Zhang, Jia1; Li, Tao1; Ge, Feng1; Zhao, Jin-dong1; Ge, F (reprint author), Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China.
2013-04-01
Source PublicationJOURNAL OF PROTEOME RESEARCH
ISSN1535-3893
Volume12Issue:4Pages:1909-1923
AbstractIncreasing 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.; 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.
SubtypeArticle
KeywordCyanobacteria Synechococcus Sp Pcc 7002 Phosphoproteomics Two-component Signaling Pathway Photosynthesis
Department[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
DOI10.1021/pr4000043
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Funding OrganizationNational Basic Research Program of China (973 Program) [2012CB518700]; National Natural Science Foundation of China [31000113]; Hundred Talents Program of the Chinese Academy of Sciences ; 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 ; 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 ; 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
Indexed BySCI
Language英语
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemical Research Methods
WOS IDWOS:000317327500034
WOS KeywordTANDEM MASS-SPECTROMETRY ; PROTEIN-PHOSPHORYLATION ; SIGNAL-TRANSDUCTION ; STATE TRANSITIONS ; SER/THR/TYR PHOSPHOPROTEOME ; PEPTIDE IDENTIFICATION ; INTERACTION NETWORKS ; BACTERIAL PROTEINS ; KINASES ; SYSTEMS
Funding OrganizationNational Basic Research Program of China (973 Program) [2012CB518700]; National Natural Science Foundation of China [31000113]; Hundred Talents Program of the Chinese Academy of Sciences ; 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 ; 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 ; 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
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Cited Times:52[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/19338
Collection水生生物分子与细胞生物学研究中心_期刊论文
Corresponding AuthorGe, F (reprint author), Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China.
Affiliation1.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100039, Peoples R China
Recommended Citation
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.,...&Ge, F .(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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