A cytoplasmic coiled‐coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1

Wei, Tao; Malone, Cheryl L.; Ault, Addison; Deschenes, Robert J.; Fassler, Jan S.

doi:10.1046/j.1365-2958.2002.02757.x

Cited by 51 publications

(59 citation statements)

References 61 publications

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“…This region (between residue 147 and residue 168) is predicted to have a high propensity for coiled-coil structure, a structure commonly found in other histidine kinases (13). Because of the dynamic nature of the helices, these coiled-coil structures might be used as a structural relay by sensing the conformational changes in the sensor domain upon the binding of a ligand and communicating this signal to the kinase core (26). Mutations in the linker region of Sln1P increase the activity of this kinase (26), as do similar mutations in NarX (10).…”

Section: Discussionmentioning

confidence: 99%

A Unique GTP-Dependent Sporulation Sensor Histidine Kinase in Bacillus anthracis

et al. 2009

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The Bacillus anthracis BA2291 gene codes for a sensor histidine kinase involved in the induction of sporulation. Genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay. Evidence suggests that the sensor domains inhibit BA2291 by titrating its activating signal ligand. Studies with purified BA2291 revealed that this kinase is uniquely specific for GTP in the forward reaction and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP-specific histidine kinases, and modeling this motif in the structure of the kinase catalytic domain suggested how guanine binds to the region. A mutation in the putative coiled-coil linker between the sensor domain and the catalytic domains was found to decrease the rate of the forward autophosphorylation reaction and not affect the reverse reaction from phosphorylated Spo0F. The results suggest that the activating ligand for BA2291 is a critical signal for sporulation and in a limited concentration in the cell. Decreasing the response to it either by slowing the forward reaction through mutation or by titration of the ligand by expressing the plasmid-encoded sensor domains switches BA2291 from an inducer to an inhibitor of the phosphorelay and sporulation.

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Section: Discussionmentioning

confidence: 99%

A Unique GTP-Dependent Sporulation Sensor Histidine Kinase in Bacillus anthracis

et al. 2009

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“…The F220D mutation in helix II of either the EnvZ, Tez1, or Tez1A1 linker causes an OmpC c phenotype in all cases, implying that mutations at helix II of the linker alter the helical orientation of the predicted coiled-coil structure so that the enzymatic functions of the downstream catalytic domain of EnvZ can no longer be modulated by external signals. It has been shown that signal transduction in several receptor proteins is regulated by altering the coiled-coil orientation (20,35).…”

Section: Discussionmentioning

confidence: 99%

Analysis of the Role of the EnvZ Linker Region in Signal Transduction Using a Chimeric Tar/EnvZ Receptor Protein, Tez1

Zhu

Inouye

2003

Journal of Biological Chemistry

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Tez1 is a chimeric protein in which the periplasmic and transmembrane domains of Tar, a chemosensor, are fused to the cytoplasmic catalytic domain of EnvZ, an osmosensing histidine kinase, through the EnvZ linker. Unlike Taz1 (a similar hybrid with the Tar linker), Tez1 could not respond to Tar ligand, aspartate, whereas single Ala insertion at the transmembrane/linker junction, as seen in Tez1A1, restored the aspartate-regulatable phenotype. Analysis of the Ala insertion site requirement and the nature of the insertion residue on the phenotype of Tez1 indicated that a junction region between the transmembrane domain and the predicted helix I in the linker is critical to signal transduction. Random mutagenesis revealed that P185Q mutation in the Tez1 linker restored the aspartate-regulatable phenotype. Substitution mutations at Pro-185 further demonstrated that specific residues are required at this site for an aspartate response. None of the hybrid receptors constructed with different Tar/EnvZ fusion sites in the linker could respond to aspartate, suggesting that specific interactions between the two predicted helices in the linker are important for the linker function. In addition, a mutation (F220D) known to cause an OmpC c phenotype in EnvZ resulted in similar OmpC c phenotypes in both Tez1A1 and Tez1, indicating the importance of the predicted helix II in signal propagation. Together, we propose that the N-terminal junction region modulates the alignment between the two helices in the linker upon signal input. In turn helix II propagates the resultant conformational signal into the downstream catalytic domain of EnvZ to regulate its bifunctional enzymatic activities.EnvZ, a histidine kinase osmosensor, locates on the inner membrane of Escherichia coli. It is composed of a periplasmic domain, transmembrane domains, and a cytoplasmic domain (1, 2). The cytoplasmic domain has been further dissected into three subdomains, the linker region, domain A, and domain B, in which the latter two form the catalytic core of EnvZ, harboring both kinase and phosphatase functions (3). NMR structures of both domain A and domain B have been solved (4, 5). Biochemical analysis has revealed that the domain A of the EnvZ is responsible for the dimerization, phosphotransfer and phosphatase functions, and domain B binds ATP and catalytically assists the enzymatic function of domain A (3, 6). The spatial arrangement between these two domains appears to be crucial for the modulation of EnvZ enzymatic activities (6). Previous studies suggest that EnvZ senses the extracellular osmolarity changes, transmits the signal through its transmembrane domain, and then modulates the kinase/phosphatase ratio of the cytoplasmic catalytic domain, which controls the cellular concentration of phosphorylated OmpR to mediate the reciprocal expression of the two major outer membrane porin proteins OmpF and OmpC (2, 7-11).Although the exact ligand for EnvZ remains unknown, two kinds of chimeric receptors have been constructed in which the periplasmic an...

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“…This domain is often found in proteins involved in the signaling system of prokaryotes, and the proteins are called HAMP (Histidine kinase, Adenyl cyclase, Methyl accepting chemotaxis protein, Phosphatase). Studies have shown that the HAMP domain is important in relation to the role of the sensor kinase, and is involved in intermolecular interactions (Pollard et al, 2009;Swain & Falke, 2007;Tao et al, 2002). In N. crassa, B. cinerea and C. heterostrophus, the deletions of the HAMP domain or amino acid-substituted mutations resulted in hyper-osmosensitivity and fungicide resistance, clearly indicating that this domain is essential for the function of Group III HisK (Cui et al, 2002;Ochiai et al, 2001;Yoshimi et al, 2004).…”

Section: Group-iii Hisk and Its Role In Filamentous Fungimentioning

confidence: 99%

Two-Component Signaling System in Filamentous Fungi and the Mode of Action of Dicarboximide and Phenylpyrrole Fungicides

Tanaka¹,

Izumitsu²

2010

Fungicides

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A cytoplasmic coiled‐coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1

Cited by 51 publications

References 61 publications

A Unique GTP-Dependent Sporulation Sensor Histidine Kinase in Bacillus anthracis

A Unique GTP-Dependent Sporulation Sensor Histidine Kinase in Bacillus anthracis

Analysis of the Role of the EnvZ Linker Region in Signal Transduction Using a Chimeric Tar/EnvZ Receptor Protein, Tez1

Two-Component Signaling System in Filamentous Fungi and the Mode of Action of Dicarboximide and Phenylpyrrole Fungicides

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