Abstract
Many different bacterial responses to environmental stimuli are controlled by pairs of proteins that act in concert and, in the aggregate, form two large families of homologous signal transduction proteins. A particular homologous domain is characteristic of each family of signal transducers: the first of these is a domain with protein kinase activity. In some instances this domain also contains a phosphoprotein phosphatase activity. The second type of conserved domain acts as the substrate for these kinase and phosphatase activities. In some cases this domain also contains an autophosphatase activity and/or it may be subject to the activity of an additional phosphatase. Information on the environment is transmitted to the kinase/phosphatase domain, which then catalyzes the phosphorylation or dephosphorylation of its substrate. Cells have evolved to use the phosphorylation and dephosphorylation of this second type of domain to regulate responses to the environmental condition by fusion of this domain to proteins, such as transcription factors, whose activity directly affects adaptive responses. Because the systems regulated in this fashion each contain at least one kinase/phosphatase and its substrate, they have been called “two-component” regulatory systems (1,2). In this review, I will refer to the kinase/phosphatase component as the kinase (K), and I will refer to the substrates for these proteins as response regulators (RR).
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Ninfa, A.J. (1991). Protein Phosphorylation and the Regulation of Cellular Processes by the Homologous Two-Component Regulatory Systems of Bacteria. In: Setlow, J.K. (eds) Genetic Engineering. Genetic Engineering, vol 13. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3760-1_2
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