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Chapter 33 : Two-Component Systems, Phosphorelays, and Regulation of Their Activities by Phosphatases

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Abstract:

Two-component systems and phosphorelays are major mechanisms by which microorganisms sense environmental stimuli and respond by gene activation and other means. Phosphorelays are used where several signals impinge on the regulatory pathway and, in the sporulation phosphorelay, at least, where the flow through the pathway is subject to several phosphatases acting on the response regulator domains. While multidomain kinases and phosphorelays are rare in bacteria, they are the rule in eukaryotes; two-component systems and CheA-like kinases are not found in eukaryotes. The original compilation of two-component systems in categorized the systems on the basis of homology of the DNA-binding domains of the response regulator. The two largest families of two-component systems are the OmpR (class III) and NarL (class II) families based on the structures of their DNA-binding domains. is the only gram-positive obligate anaerobe whose genome has been fully sequenced to date. In the phosphorelay, two families of phosphatases, the Rap and the SpoOE families, specifically dephosphorylate the SpoOF~P and SpoOA~P response regulators, respectively. These phosphatases are differentially induced by physiological conditions antithetical to sporulation, such as those conditions that promote growth or competence to DNA transformation. The competition between signal input provided by the kinases and signal cancellation carried out by the phosphatases determines the final output of the system and therefore whether or not the cell will initiate the process of sporulation.

Citation: Perego M, Hoch J. 2002. Two-Component Systems, Phosphorelays, and Regulation of Their Activities by Phosphatases, p 473-481. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch33

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Two-Component Signal Transduction Systems
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Figures

Image of FIGURE 1
FIGURE 1

Pathway of phosphoryl transfer in a two-component system. Signal ligand binding by the signal input domain of the kinase induces the autokinase to hydrolyze ATP and autophosphory-late a histidine residue. Phosphoryl transfer to the response regulator involves specific molecular interaction between the autokinase and the regulator domain of the response regulator, resulting in the phosphorylation of an aspartic acid residue. The phosphorylation of the aspartate activates or disin-hibits the function of the output domain.

Citation: Perego M, Hoch J. 2002. Two-Component Systems, Phosphorelays, and Regulation of Their Activities by Phosphatases, p 473-481. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch33
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Image of FIGURE 2
FIGURE 2

Domain organization of two-component and phosphorelay systems. Signaling domains (S) differ in size, sequence, and/or structure in histidine kinases. The usual two-component system (top) consists of the phosphotransferase domain (PT), an ATP-binding domain (ATP), a regulator domain (R), and an output domain (O) in addition to the signal domain(s). The chemotaxis system consists of a membrane-bound signaling domain (MCP), a kinase consisting of a phosphotransferase domain (HpT) and an ATP-binding domain, and a regulator/output domain (R/O). HpT domains are four-helix bundles produced from a single polypeptide chain, whereas PT domains contain four-helix bundles produced by dimerization of two helices from each protomer. Both PT and kinase domains are dimers. The sporulation phosphorelay of Bacillus subtilis and the BvgS/A phosphorelay of Bordetella pertussis use the same pathway of phosphoryl transfer whether the domains are single proteins or connected in a poly-domain protein.

Citation: Perego M, Hoch J. 2002. Two-Component Systems, Phosphorelays, and Regulation of Their Activities by Phosphatases, p 473-481. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch33
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Image of FIGURE 3
FIGURE 3

Amino acid sequence alignment of Rap phosphatases derived from genome sequences. The RapA protein from ( ) was aligned with the five orthologues identified in the genome sequence (Bhalo) ( ), and three were identified in (Banth) (http://www.tigr.org) using Clustal W. The six predicted TPR motifs are shaded in gray ( ). Identical residues are marked by an asterisk, and conserved residues are identified by a colon.

Citation: Perego M, Hoch J. 2002. Two-Component Systems, Phosphorelays, and Regulation of Their Activities by Phosphatases, p 473-481. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch33
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Image of FIGURE 4
FIGURE 4

Amino acid sequence alignment of phosphatases belonging to the Spo0E family. The Spo0E, YisI, and YnzD proteins ( ) were aligned by Clustal W with the four orthologues identified in the genome sequence of (http://www.tigr.org), the four identified in B. halodurans ( ), and the one identified in B. stearothermophilus (http://www.genome.ou.edu) and B. cereus (http://wit.integratedgenomics. com). Identical residues are indicated by an asterisk, and conserved substitutions are marked by a colon. The region containing the signature sequence for the Spo0F-like phosphatases is shaded in gray.

Citation: Perego M, Hoch J. 2002. Two-Component Systems, Phosphorelays, and Regulation of Their Activities by Phosphatases, p 473-481. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch33
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Tables

Generic image for table
TABLE 1

Two-component systems in

Classes defined by comparing the kinase sequences around the phosphorylatable histidine.

Families of two-component systems defined in by comparing the response regulator C-terminal domains.

Organization of each pair of kinase/regulator on the chromosome (HR, 5′ histidine kinase-3′ response regulator; RH, 5′ response regulator-3′ histidine kinase).

“Orphan” designates a histidine kinase gene that is not directly associated with a response regulator gene in an operon on the chromosome.

YkvD and YkrQ are now designated KinD and KinE, respectively.

Citation: Perego M, Hoch J. 2002. Two-Component Systems, Phosphorelays, and Regulation of Their Activities by Phosphatases, p 473-481. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch33

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