D-乳酸对大肠杆菌中ArcB传感器激酶生理活性的影响。
Effect of D-lactate on the physiological activity of the ArcB sensor kinase in Escherichia coli.
作者信息
Rodriguez Claudia, Kwon Ohsuk, Georgellis Dimitris
机构信息
Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, 04510 Mexico City, Mexico.
出版信息
J Bacteriol. 2004 Apr;186(7):2085-90. doi: 10.1128/JB.186.7.2085-2090.2004.
Abstract
The Arc two-component system, comprising the ArcB sensor kinase and the ArcA response regulator, modulates the expression of numerous genes in response to the respiratory growth conditions. Under anoxic growth conditions ArcB autophosphorylates and transphosphorylates ArcA, which in turn represses or activates its target operons. The anaerobic metabolite D-lactate has been shown to stimulate the in vitro autophosphorylating activity of ArcB. In this study, the in vivo effect of D-lactate on the kinase activity of ArcB was assessed. The results demonstrate that D-lactate does not act as a direct signal for activation of ArcB, as previously proposed, but acts as a physiologically significant effector that amplifies ArcB kinase activity.
摘要
由ArcB传感激酶和ArcA应答调节因子组成的双组分系统Arc，可根据呼吸生长条件调节众多基因的表达。在缺氧生长条件下，ArcB会自动磷酸化并将磷酸基团转移给ArcA，进而抑制或激活其靶操纵子。研究表明，厌氧代谢物D-乳酸可刺激ArcB的体外自动磷酸化活性。在本研究中，评估了D-乳酸对ArcB激酶活性的体内影响。结果表明，D-乳酸并非如先前提出的那样作为激活ArcB的直接信号，而是作为一种具有生理意义的效应物，可放大ArcB激酶活性。
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