Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002.
Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002.
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DOI：
10.1021/pr4000043
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发表时间：
2013-03
影响因子：
4.4
通讯作者：
Mingkun Yang;Zhi-Xian Qiao;Wan-yi Zhang;Qian Xiong;Jia Zhang;Tao Li;F. Ge;Jindong Zhao
中科院分区：
文献类型：
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作者：
Mingkun Yang;Zhi-Xian Qiao;Wan-yi Zhang;Qian Xiong;Jia Zhang;Tao Li;F. Ge;Jindong Zhao
越来越多的证据表明，丝氨酸（Ser），苏氨酸（Thr）和酪氨酸（Tyr）残基上的蛋白磷酸化是细菌中主要的翻译后修饰之一，参与调节无数的生理过程。蓝藻是细菌中最大的类群之一，也是唯一能够进行光合作用的原核生物。许多蓝细菌菌株含有异常高数量的蛋白激酶和磷酸酶，对Ser、Thr和Tyr残基具有特异性。然而，只有几十个磷酸化位点在蓝藻是已知的，提出了一个主要的障碍，进一步了解可逆磷酸化在这组细菌的调节作用。在这项研究中，我们进行了一个全球性的和位点特异性的磷酸蛋白质组学分析的模式蓝藻聚球藻7002。通过蛋白质/肽预分离、TiO 2富集和LC-MS/MS分析，共鉴定了245种聚球藻PCC 7002蛋白的280个磷酸肽和410个磷酸化位点。这些磷蛋白在功能上被归类为相互作用图谱，并被发现参与各种生物过程，如双组分信号通路和光合作用。我们的数据提供了第一个全球调查的磷酸化蓝藻通过使用磷酸化蛋白质组学的方法，并提出了广泛的监管范围内的这种修改。所提供的数据集可能有助于揭示潜在的Ser/Thr/Tyr磷酸化的生理功能，并有助于阐明蓝藻中的整个信号网络。
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.