Proteome Center Tuebingen, University of Tuebingen, Germany.
Proteomics. 2011 Aug;11(15):3002-11. doi: 10.1002/pmic.201100012. Epub 2011 Jul 4.
Protein phosphorylation on serine, threonine and tyrosine is established as an important regulatory modification in bacteria. A growing number of studies employing mass spectrometry-based proteomics report large protein phosphorylation datasets, providing precise evidence for in-vivo phosphorylation that is especially suitable for functional follow-up. Here, we provide an overview of the strategies currently used in bacterial phosphoproteomics, with an emphasis on gel-free proteomics and approaches that enable global detection of phosphorylation sites in bacterial proteins. The proteomics technology has matured sufficiently to permit routine characterization of phosphoproteomes and phosphopeptides with high sensitivity; we argue that the next challenge in the field will be the large-scale detection of protein kinase and phosphatase substrates and their integration into regulatory networks of the bacterial cell.
丝氨酸、苏氨酸和酪氨酸的蛋白质磷酸化被确定为细菌中一种重要的调节修饰方式。越来越多的基于质谱的蛋白质组学研究报告了大量的蛋白质磷酸化数据集，为体内磷酸化提供了精确的证据，特别适合功能后续研究。在这里，我们提供了目前在细菌磷酸蛋白质组学中使用的策略概述，重点介绍了无胶蛋白质组学和能够全局检测细菌蛋白质中磷酸化位点的方法。蛋白质组学技术已经成熟到足以允许用高灵敏度常规表征磷酸蛋白质组和磷酸肽；我们认为该领域的下一个挑战将是大规模检测蛋白激酶和磷酸酶的底物，并将其整合到细菌细胞的调控网络中。
