Journal of Molecular Biology
Regular ArticleLigand Binding to the Receptor Domain Regulates the Ratio of Kinase to Phosphatase Activities of the Signaling Domain of the Hybrid Escherichia coli Transmembrane Receptor, Taz1
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Molecular Mechanisms of Two-Component Signal Transduction
2016, Journal of Molecular BiologyCytoplasmic sensing by the inner membrane histidine kinase EnvZ
2015, Progress in Biophysics and Molecular BiologyCitation Excerpt :In some two-component signaling systems, dephosphorylation of the phosphorylated RR via the HK (the so-called “phosphatase activity”) limits the level of the activated RR and serves to reset the system. Although it was proposed that EnvZ phosphatase activity was reduced in the presence of high osmolality (Jin and Inouye, 1993), Fig. 3 clearly shows that high osmolality leads to a direct effect on EnvZ activation via autophosphorylation (Wang et al., 2012). These results are consistent with ATPase measurements of EnvZ-stimulated OmpR ∼ P dephosphorylation at in-vivo ratios of EnvZ to OmpR (Kenney, 2010).
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2010, Current Opinion in MicrobiologyCitation Excerpt :The level of Taz1 was estimated to be ∼20-fold higher than normal EnvZ levels. Both Taz1 autophosphorylation and phosphotransfer to OmpR were not affected by aspartate, but extremely small aspartate-induced decreases in phosphatase activity were observed [49]. A concern about the physiological relevance of the aspartate response mediated by Taz1 is that, in contrast to Tar, Taz1 requires very high concentrations of aspartate to stimulate ompC-lacZ expression.