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Two-Component Systems in Plant Signal Transduction Takeshi Urao, Kazuko Yamaguchi-Shinozaki and Kazuo Shinozaki

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Two-Component Systems in Plant Signal Transduction Takeshi Urao, Kazuko Yamaguchi-Shinozaki and Kazuo Shinozaki trends in plant science Reviews Two-component systems in plant signal transduction Takeshi Urao, Kazuko Yamaguchi-Shinozaki and Kazuo Shinozaki In plants, two-component systems play important roles in signal transduction in response to environmental stimuli and growth regulators. Genetic and biochemical analyses indicate that sensory hybrid-type histidine kinases, ETR1 and its homologs, function as ethylene re- ceptors and negative regulators in ethylene signaling. Two other hybrid-type histidine kinases, CKI1 and ATHK1, are implicated in cytokinin signaling and osmosensing processes, respectively. A data base search of Arabidopsis ESTs and genome sequences has identified many homologous genes encoding two-component regulators. We discuss the possible origins and functions of these two-component systems in plants. ll living organisms have diverse and sophisticated signal- A multistep His-to-Asp phosphorelay: more than ing strategies to recognize and respond to their environ- two components Amental conditions. Protein phosphorylation is a key Such a simple His-to-Asp phosphorelay is not the only two-com- mechanism for intracellular signal transduction in both eukaryotic ponent system. In some cases, two-component systems include and prokaryotic cells. This process is catalyzed by protein additional signaling modules or motifs and constitute more kinases, and these are classified into three major groups based on complicated phosphorelay circuits (Fig. 1). This additional signal- their substrate specificities: serine/threonine kinases, tyrosine ing domain, known as the histidine-containing phosphotransfer kinases and histidine kinases. Histidine kinases in bacteria play (HPt) domain, was first uncovered in an E. coli anaerobic sensor key roles in sensing and transducing extracellular signals in- ArcB. For instance, an osmosensory two-component system in cluding chemotactic factors, changes in osmolarity, and nutrient Saccharomyces cerevisiae consists of three signaling molecules, deficiency. This signal transduction system is mediated by SLN1, YPD1 and SSK1 (Ref. 3). The histidine kinase SLN1 acts phosphotransfer between two types of signal transducers and is as a transmembrane osmosensor. SLN1 has both a kinase and a therefore referred to as the ‘two-component system’1. The two- receiver domain within the same molecule. This type of histidine component system has been well defined in bacteria, and, in kinase is referred to as ‘hybrid histidine kinase’. At normal osmo- 1993, the existence of a bacterial-type histidine kinase was re- larity, SLN1 is activated to autophosphorylate a histidine residue ported in yeast and in Arabidopsis2,3. Since then, many genes within the kinase domain using ATP as a phosphodonor. The encoding two-component regulators have been identified in phosphoryl group is transferred sequentially by a phosphorelay plants, yeast and Dictyostelium3,4. However, the existence of two- reaction to an aspartate residue within the receiver domain, and component regulators in animals has not been reported. In this then to a histidine residue in the intermediary molecule YPD1, review, we focus on the two-component regulators and their and finally to an aspartate residue within the receiver domain of function in plants. the response regulator SSK1. The phosphorylated form of SSK1 is incapable of activating an osmosensing HOG1 MAPK cascade. A simple His-to-Asp phosphorelay: two components By contrast, under conditions of high osmolarity, SLN1 is inacti- Typically, the two-component system is composed of a sensory vated, enabling unphosphorylated SSK1 to accumulate, which histidine kinase and a response regulator (Fig. 1). The histidine leads to the activation of the HOG1 MAPK cascade. A similar sig- kinase contains an N-terminal input domain and a C-terminal naling system also operates in osmosensing in fission yeast. The kinase domain with an invariant histidine residue. The response response regulator MCS4 regulates a WAK1-WIS1-STY1 MAPK regulator contains an N-terminal receiver domain with an in- pathway in Schizosaccharomyces pombe5. Such a multistep phos- variant aspartate residue and a C-terminal output domain. For phorelay reaction is believed to have the potential advantages of example, in E. coli, osmotic responses are controlled by an providing multiple regulatory checkpoints for signal cross-talk or EnvZ–OmpR two-component system. The input domain of the negative regulation by certain phosphatases. Multistep phospho- sensory histidine kinase EnvZ somehow detects changes in exter- relays are known to be involved in anaerobic regulation in E. coli, nal osmolarity and modulates intrinsic kinase and phosphatase in sporulation in Bacillus subtilis, and in virulence control in activities. High osmolarity promotes autophosphorylation of a Bordetella pertussis. The existence of multistep phosphorelay histidine residue within its kinase domain, followed by transfer reactions in both prokaryotes and eukaryotes suggests that similar of the phosphoryl group to an aspartate residue within the mechanisms might be more widely used. receiver domain of the cognate response regulator OmpR. By contrast, low osmolarity promotes dephosphorylation of the Link between prokaryotic two-component system phosphorylated OmpR. The phosphorylation state of OmpR and eukaryotic signal transduction system alters the DNA-binding activity of the output domain to control The best documented linkage between prokaryotic and eukaryotic the transcription of target genes. Thus, a physical signal (e.g. two-component signal transduction mechanisms is for the an environmental stimulus) can be converted to a biochemical osmoregulation systems of yeast. As mentioned already, in reaction, termed ‘His-to-Asp phosphorelay’, by two-component S. cerevisiae, exposure to high osmolarity activates the HOG1 signaling systems. MAPK cascade through the SLN1-YPD1-SSK1 two-component 1360 - 1385/00/$ – see front matter © 2000 Elsevier Science Ltd. All rights reserved. PII: S1360-1385(99)01542-3 February 2000, Vol. 5, No. 2 67 trends in plant science Reviews system. At high osmolarity, the unphosphorylated response Histidine Phosphorelay Response regulator SSK1 activates SSK2 and SSK22 (MAPKKK) by direct kinase intermediate regulator protein–protein interaction. The activated SSK2 and SSK22 phos- phorylates PBS2 (MAPKK), and HOG1 (MAPK) is activated. (a) Furthermore, it should be noted that, in addition to SLN1, another P P osmosensor, SHO1, is known in budding yeast3. SHO1 is not a H D member of the two-component family, but it acts as a transmem- EnvZ OmpR brane osmosensor, activating PBS2 MAPKK by direct interaction between the SH3 domain of SHO1 and the proline-rich region (b) of PBS2. SLN1 and SHO1 appear to have a different salt concen- P P P P tration dependency and a different time course for providing an optimal response to osmolarity changes. In yeast, multiple MAPK H D H D cascades are involved in the responses to a variety of external YPD1 SSK1 SLN1 stimuli. For example, STE11 (MAPKKK) shares two independent Trends in Plant Science pathways, an osmosensing SHO1–HOG1 pathway and a pheromone- Fig. 1. Two types of phosphorelay signaling in two-component response FUS3/KSS1 pathway. Nevertheless,osmotic stress, which systems. The input domain is depicted in pink, the transmembrane leads to the activation of the HOG1 MAPK cascade, never acti- region in grey, the kinase domain in blue, the receiver domain in vates the FUS3/KSS1 MAPK cascade. Thus, the two pathways light green, the histidine-containing phosphotransfer domain in respond to a specific signal, and function independently. This dark green and the output domain in purple. H represents histidine functional separation is achieved by a scaffold protein that prevents and D represents aspartate. (a) Single step His-to-Asp phospho- undesirable signals entering and interfering with the pathway. In relay. The sensory kinase EnvZ recognizes a high osmolarity con- dition and autophosphorelates a histidine residue in the kinase any event, it should be emphasized that the prokaryotic-like two- domain. The phosphoryl group is then transferred to an aspartate component signaling mechanism can be linked downstream to typi- residue in the receiver domain of the response regulator OmpR. cal eukaryotic (MAPK) signaling cascades, in yeast. This intriguing The phosphorylated OmpR promotes its DNA-binding activity view is further supported by recent findings that two-component and activates the transcription of high osmolarity-responsive systems in Dictyostelium play important roles in signal recognition genes. (b) Multistep His-to-Asp phosphorelay. Under conditions and development, as described below. of high osmolarity, the sensory kinase SLN1 autophosphorylates A gene, dokA, encoding a hybrid histidine kinase has been and blocks the activation of the osmoregulatory HOG1 MAPK cloned from Dictyostelium6. The dokA deletion mutants show a cascade through a multistep phosphorelay between an aspartate dramatic reduction in viability after exposure to medium of high residue in the receiver domain, a histidine residue in the phos- osmolarity and inhibition of growth and development under less phorelay intermediate YPD1, and an aspartate residue in the receiver domain of the response regulator SSK1. By contrast, high stringent osmolarity conditions. DokA, unlike EnvZ and SLN1, osmolarity inactivates SLN1, resulting in the accumulation of does not contain extensive hydrophobic regions, suggesting a unphosphorylated SSK1. soluble
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