Gudipaty Swapna A, McEvoy Megan M
Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA; Department of Soil, Water and Environmental Sciences, University of Arizona, Tucson, AZ 85721, USA.
Biochim Biophys Acta. 2014 Sep;1844(9):1656-61. doi: 10.1016/j.bbapap.2014.06.001. Epub 2014 Jun 16.
The Cus system of Escherichia coli aids in protection of cells from high concentrations of Ag(I) and Cu(I). The histidine kinase CusS of the CusRS two-component system functions as a Ag(I)/Cu(I)-responsive sensor kinase and is essential for induction of the genes encoding the CusCFBA efflux pump. In this study, we have examined the molecular features of the sensor domain of CusS in order to understand how a metal-responsive histidine kinase senses specific metal ions. We find that the predicted periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. These findings suggest a model for activation of the histidine kinase through metal binding events in the periplasmic sensor domain.
大肠杆菌的Cus系统有助于保护细胞免受高浓度Ag(I)和Cu(I)的侵害。CusRS双组分系统的组氨酸激酶CusS作为Ag(I)/Cu(I)响应传感器激酶发挥作用,对于诱导编码CusCFBA外排泵的基因至关重要。在本研究中,我们研究了CusS传感器结构域的分子特征,以了解金属响应组氨酸激酶如何感知特定金属离子。我们发现,预测的CusS周质传感器结构域直接与Ag(I)离子相互作用,并在金属结合时发生构象变化。金属结合还增强了该结构域二聚化的倾向。这些发现提示了一种通过周质传感器结构域中的金属结合事件激活组氨酸激酶的模型。