Department of Microbiology & Immunology, University of Illinois at Chicago, 835 S. Wolcott St. M/C 790, Chicago, IL 60612, USA.
Curr Opin Microbiol. 2010 Apr;13(2):168-76. doi: 10.1016/j.mib.2010.01.013. Epub 2010 Mar 10.
In two-component signaling systems, phosphorylated response regulators (RRs) are often dephosphorylated by their partner kinases in order to control the in vivo concentration of phospho-RR (RR approximately P). This activity is easily demonstrated in vitro, but these experiments have typically used very high concentrations of the histidine kinase (HK) compared to the RR approximately P. Many two-component systems exhibit exquisite control over the ratio of HK to RR in vivo. The question thus arises as to whether the phosphatase activity of HKs is significant in vivo. This topic will be explored in the present review.
在双组分信号系统中,磷酸化的反应调节蛋白(RR)通常会被其伴侣激酶去磷酸化,以控制磷酸化 RR(RRP)的体内浓度。这种活性在体外很容易被证明,但这些实验通常使用比 RRP 高得多的组氨酸激酶(HK)浓度。许多双组分系统在体内对 HK 与 RR 的比例表现出精确的控制。因此,问题就出现了:HK 的磷酸酶活性在体内是否重要。本综述将探讨这一主题。