Yaku H, Kato M, Hakoshima T, Tsuzuki M, Mizuno T
Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Japan.
FEBS Lett. 1997 May 26;408(3):337-40. doi: 10.1016/s0014-5793(97)00459-6.
Bacteria have devised sophisticated His-Asp phosphorelay signaling systems for eliciting a variety of adaptive responses to their environment. The histidine-containing phosphotransfer (HPt) domain, found in many signal transduction protein, functions as a mediator of the His-Asp phosphorelay. The ArcB anaerobic sensor of E. coli contains such a HPt domain, although its function is not fully understood. In this study, we provide in vivo and in vitro evidence that the HPt domain is capable of interacting with the CheY receiver, which contains a phospho-accepting aspartate residue.
细菌已经设计出复杂的组氨酸-天冬氨酸磷酸转移信号系统，以引发对其环境的多种适应性反应。在许多信号转导蛋白中发现的含组氨酸的磷酸转移（HPt）结构域，作为组氨酸-天冬氨酸磷酸转移的介质发挥作用。大肠杆菌的ArcB厌氧传感器含有这样一个HPt结构域，尽管其功能尚未完全了解。在本研究中，我们提供了体内和体外证据，证明该HPt结构域能够与CheY受体相互作用，CheY受体含有一个磷酸接受天冬氨酸残基。
