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Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics
Nature Methods ( IF 48.0 ) Pub Date : 2018-01-29 , DOI: 10.1038/nmeth.4580 Clement M Potel , Miao-Hsia Lin , Albert J R Heck , Simone Lemeer
中文翻译:
基于质谱的蛋白质组学揭示了广泛的细菌蛋白组氨酸磷酸化
更新日期:2018-01-29
Nature Methods ( IF 48.0 ) Pub Date : 2018-01-29 , DOI: 10.1038/nmeth.4580 Clement M Potel , Miao-Hsia Lin , Albert J R Heck , Simone Lemeer
For decades, major difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in Escherichia coli. We generated an extensive E. coli phosphoproteome data set, in which a remarkably high percentage (∼10%) of phosphorylation sites are phosphohistidine sites. This resource should help enable a better understanding of the biological function of histidine phosphorylation.
中文翻译:
基于质谱的蛋白质组学揭示了广泛的细菌蛋白组氨酸磷酸化
几十年来,分析组氨酸磷酸化的主要困难限制了磷酸组氨酸信号转导的研究。在这里我们报告的一种方法揭示了大肠杆菌中广泛而丰富的蛋白组氨酸磷酸化。我们生成了广泛的大肠杆菌磷酸化蛋白质组数据集,其中磷酸化位点的百分比很高(约10%)是磷酸组氨酸位点。该资源应有助于更好地了解组氨酸磷酸化的生物学功能。