Faculty Opinions recommendation of The β-scaffold of the LOV domain of the Brucella light-activated histidine kinase is a key element for signal transduction.

2012 ◽  
Author(s):  
Ann Stock
Keyword(s):  
Signal Transduction ◽  
Histidine Kinase ◽  
Lov Domain

The β-Scaffold of the LOV Domain of the Brucella Light-Activated Histidine Kinase Is a Key Element for Signal Transduction

2012 ◽  
Vol 420 (1-2) ◽  
pp. 112-127 ◽  
Author(s):  
Jimena Rinaldi ◽  
Mariana Gallo ◽  
Sebastián Klinke ◽  
Gastón Paris ◽  
Hernán R. Bonomi ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Histidine Kinase ◽  
Lov Domain

scholarly journals PAS-mediated Dimerization of Soluble Guanylyl Cyclase Revealed by Signal Transduction Histidine Kinase Domain Crystal Structure

2007 ◽  
Vol 283 (2) ◽  
pp. 1167-1178 ◽  
Author(s):  
Xiaolei Ma ◽  
Nazish Sayed ◽  
Padmamalini Baskaran ◽  
Annie Beuve ◽  
Focco van den Akker
Keyword(s):  
Crystal Structure ◽  
Signal Transduction ◽  
Guanylyl Cyclase ◽  
Histidine Kinase ◽  
Soluble Guanylyl Cyclase ◽  
Kinase Domain

Kinetic and mechanistic analyses of new classes of inhibitors of two-component signal transduction systems using a coupled assay containing HpkA–DrrA from Thermotoga maritima

Microbiology ◽  
2004 ◽  
Vol 150 (4) ◽  
pp. 885-896 ◽  
Author(s):  
J. Estelle Foster ◽  
Qin Sheng ◽  
Jonathan R. McClain ◽  
Mark Bures ◽  
Thalia I. Nicas ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Histidine Kinase ◽  
Competitive Inhibition ◽  
Thermotoga Maritima ◽  
Phosphorylation Site ◽  
Phosphoryl Group ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Coupled Assay ◽  
Signal Transduction Systems

Two-component signal transduction systems (TCSs) play fundamental roles in bacterial survival and pathogenesis and have been proposed as targets for the development of novel classes of antibiotics. A new coupled assay was developed and applied to analyse the kinetic mechanisms of three new kinds of inhibitors of TCS function. The assay exploits the biochemical properties of the cognate HpkA–DrrA histidine kinase–response regulator pair from Thermotoga maritima and allows multiple turnovers of HpkA, linear formation of phosphorylated DrrA, and Michaelis–Menten analysis of inhibitors. The assay was validated in several ways, including confirmation of competitive inhibition by adenosine 5′-β,γ-imidotriphosphate (AMP-PNP). The coupled assay, autophosphorylation and chemical cross-linking were used to determine the mechanisms by which several compounds inhibit TCS function. A cyanoacetoacetamide showed non-competitive inhibition with respect to ATP concentration in the coupled assay. The cyanoacetoacetamide also inhibited autophosphorylation of histidine kinases from other bacteria, indicating that the coupled assay could detect general inhibitors of histidine kinase function. Inhibition of HpkA autophosphorylation by this compound was probably caused by aggregation of HpkA, consistent with a previous model for other hydrophobic compounds. In contrast, ethodin was a potent inhibitor of the combined assay, did not inhibit HpkA autophosphorylation, but still led to aggregation of HpkA. These data suggest that ethodin bound to the HpkA kinase and inhibited transfer of the phosphoryl group to DrrA. A peptide corresponding to the phosphorylation site of DrrA appeared to inhibit TCS function by a mechanism similar to that of ethodin, except that autophosphorylation was inhibited at high peptide concentrations. The latter mechanism of inhibition of TCS function is unusual and its analysis demonstrates the utility of these approaches to the kinetic analyses of additional new classes of inhibitors of TCS function.

Histidine kinase activity and the regulation of ethylene signal transduction

2005 ◽  
Vol 83 (6) ◽  
pp. 563-570 ◽  
Author(s):  
Michael G Mason ◽  
G Eric Schaller
Keyword(s):  
Signal Transduction ◽  
Plant Growth ◽  
Histidine Kinase ◽  
Kinase Activity ◽  
Ethylene Receptor ◽  
Serine Threonine Kinase ◽  
Two Component ◽  
Ethylene Signal Transduction ◽  
Ethylene Signal

Ethylene is a gaseous hormone that regulates many aspects of plant growth and development. Although the effect of ethylene on plant growth was discovered a century ago, the key players in the ethylene response pathway were only identified over the last 15 years. In Arabidopsis, ethylene is perceived by a family of five receptors (ETR1, ETR2, ERS1, ERS2, and EIN4) that resemble two-component histidine kinases. Of these, only ETR1 and ERS1 contain all the conserved residues required for histidine kinase activity. The ethylene receptors appear to function primarily through CTR1, a serine/threonine kinase that actively suppresses ethylene responses in air (absence of ethylene). Despite recent progress toward understanding ethylene signal transduction, the role of the ethylene-receptor histidine-kinase activity remains unclear. This review considers the significance of histidine kinase activity in ethylene signaling and possible mechanisms by which it may modulate ethylene responses.Key words: ethylene receptor, ETR1, histidine kinase, two-component, phosphorylation, Arabidopsis.

scholarly journals The Two-Component Signal Transduction System VxrAB Positively Regulates Vibrio cholerae Biofilm Formation

2017 ◽  
Vol 199 (18) ◽  
Author(s):  
Jennifer K. Teschler ◽  
Andrew T. Cheng ◽  
Fitnat H. Yildiz
Keyword(s):  
Signal Transduction ◽  
Vibrio Cholerae ◽  
Histidine Kinase ◽  
Biofilm Formation ◽  
Pathogenic Bacteria ◽  
Response Regulator ◽  
Systematic Analysis ◽  
Content Type ◽  
Two Component ◽  
Two Component Signal Transduction

ABSTRACT Two-component signal transduction systems (TCSs), typically composed of a sensor histidine kinase (HK) and a response regulator (RR), are the primary mechanism by which pathogenic bacteria sense and respond to extracellular signals. The pathogenic bacterium Vibrio cholerae is no exception and harbors 52 RR genes. Using in-frame deletion mutants of each RR gene, we performed a systematic analysis of their role in V. cholerae biofilm formation. We determined that 7 RRs impacted the expression of an essential biofilm gene and found that the recently characterized RR, VxrB, regulates the expression of key structural and regulatory biofilm genes in V. cholerae. vxrB is part of a 5-gene operon, which contains the cognate HK vxrA and three genes of unknown function. Strains carrying ΔvxrA and ΔvxrB mutations are deficient in biofilm formation, while the ΔvxrC mutation enhances biofilm formation. The overexpression of VxrB led to a decrease in motility. We also observed a small but reproducible effect of the absence of VxrB on the levels of cyclic di-GMP (c-di-GMP). Our work reveals a new function for the Vxr TCS as a regulator of biofilm formation and suggests that this regulation may act through key biofilm regulators and the modulation of cellular c-di-GMP levels. IMPORTANCE Biofilms play an important role in the Vibrio cholerae life cycle, providing protection from environmental stresses and contributing to the transmission of V. cholerae to the human host. V. cholerae can utilize two-component systems (TCS), composed of a histidine kinase (HK) and a response regulator (RR), to regulate biofilm formation in response to external cues. We performed a systematic analysis of V. cholerae RRs and identified a new regulator of biofilm formation, VxrB. We demonstrated that the VxrAB TCS is essential for robust biofilm formation and that this system may regulate biofilm formation via its regulation of key biofilm regulators and cyclic di-GMP levels. This research furthers our understanding of the role that TCSs play in the regulation of V. cholerae biofilm formation.

scholarly journals A bacterial signal transduction phosphorelay in the methanogenic archaeon Methanosarcina acetivorans

2021 ◽  
Author(s):  
Nicole Frankenberg-Dinkel ◽  
Anne Sexauer
Keyword(s):  
Signal Transduction ◽  
Histidine Kinase ◽  
Environmental Changes ◽  
Methanosarcina Acetivorans ◽  
Histidine Kinases ◽  
C Terminus ◽  
Component Systems ◽  
Two Component Systems ◽  
Bacterial Type

Signal transduction via two-component systems is a powerful tool for microorganisms to respond to environmental changes. Histidine kinases originating from Bacteria are the most common signaling enzymes and are also present in Archaea, but not in all phyla. A total of 124 bacterial-type histidine kinases and/or regulators were identified in a screen of 149 Euryarchaeota genomes, but little is known about the signal transfer and molecular regulation of these systems. In this work, the hybrid kinase MA4377 from the methanogenic archaeon Methanosarcina acetivorans was investigated. MA4377 is a multidomain protein resembling a bacterial-type histidine kinase with two additional receiver domains at the C-terminus. Recombinant protein was employed to investigate the intra- and intermolecular phosphorelay in vitro. The kinase displays autophosphorylation activity of histidine residue 497. While no intramolecular phosphorelay was observed, the CheY-like receiver protein MA4376 was identified as part of the multi-component system that also seems to include the Msr-type transcription factor MA4375. This study reveals the presence and in vitro function of a bacterial-type hybrid histidine kinase integrated into an archaeal phosphorelay system.

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