Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis
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DOI：
10.1073/pnas.1117483109
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发表时间：
2012-05-08
影响因子：
11.1
通讯作者：
Gerth, Ulf
中科院分区：
文献类型：
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作者：
Elsholz, Alexander K. W.;Turgay, Kuersad;Gerth, Ulf
可逆性蛋白质磷酸化是所有活细胞中重要且普遍存在的蛋白质修饰。在这里，我们报告说，蛋白质磷酸化精氨酸残基起着重要的生理作用。我们在革兰氏阳性模式生物枯草芽孢杆菌体内检测到87个蛋白质中的121个精氨酸磷酸化位点。此外，我们提供的证据表明，蛋白质精氨酸磷酸化具有功能性作用，并参与调节许多关键的细胞过程，如蛋白质降解，运动，能力，严格和压力反应。我们的研究结果表明，在B。在枯草杆菌中，蛋白质精氨酸激酶和磷酸酶的组合活性允许蛋白质活性的快速和可逆调节，并且蛋白质精氨酸磷酸化可以在细菌中发挥生理学上重要的调节作用。
Reversible protein phosphorylation is an important and ubiquitous protein modification in all living cells. Here we report that protein phosphorylation on arginine residues plays a physiologically significant role. We detected 121 arginine phosphorylation sites in 87 proteins in the Gram-positive model organism Bacillus subtilis in vivo. Moreover, we provide evidence that protein arginine phosphorylation has a functional role and is involved in the regulation of many critical cellular processes, such as protein degradation, motility, competence, and stringent and stress responses. Our results suggest that in B. subtilis the combined activity of a protein arginine kinase and phosphatase allows a rapid and reversible regulation of protein activity and that protein arginine phosphorylation can play a physiologically important and regulatory role in bacteria.