Search results for "Histidine kinase"

showing 10 items of 28 documents

Visualizing fungicide action: anin vivotool for rapid validation of fungicides with target location HOG pathway

2018

BACKGROUND The mitogen-activated protein kinase MoHog1p was fused with a green fluorescent protein (GFP) in the filamentous fungus Magnaporthe oryzae. The MoHOG1::GFP mutant was found to be an excellent tool visualizing in vivo fungicide-dependent translocation of MoHog1p into the nucleus. Validation of pathway specificity was achieved by generating fluorescence-labelled MoHog1p in the ΔMohik1 'loss of function' mutant strain. RESULTS GFP-labelled MoHog1p expressed in the wildtype and in ΔMohik1 demonstrates that fludioxonil is acting on the HOG pathway and even more precisely that fungicide action is dependent on the group III histidine kinase MoHik1p. GFP-tagged MoHog1p translocated into …

0106 biological sciencesFungal proteinMagnaporthebiologyChemistryMutantHistidine kinaseWild typeGeneral Medicinebiology.organism_classification01 natural sciencesGreen fluorescent proteinCell biology010602 entomologyIn vivoInsect ScienceProtein kinase AAgronomy and Crop Science010606 plant biology & botanyPest Management Science
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Transmembrane signaling and cytoplasmic signal conversion by dimeric transmembrane helix 2 and a linker domain of the DcuS sensor kinase

2020

Transmembrane (TM) signaling is a key process of membrane-bound sensor kinases. The C4-dicarboxylate (fumarate) responsive sensor kinase DcuS of Escherichia coli is anchored by TM helices TM1 and TM2 in the membrane. Signal transmission across the membrane relies on the piston-type movement of the periplasmic part of TM2. To define the role of TM2 in TM signaling, we use oxidative Cys cross-linking to demonstrate that TM2 extends over the full distance of the membrane and forms a stable TM homodimer in both the inactive and fumarate-activated state of DcuS. An S186xxxGxxxG194 motif is required for the stability and function of the TM2 homodimer. The TM2 helix further extends on the periplas…

0301 basic medicineCytoplasmGpA glycophorin AC4DC C4-dicarboxylateCL cross-linkingpiston-typeMBP maltose-binding proteinBiochemistry03 medical and health sciencesProtein DomainsDcuSEscherichia coli(Gly)xxx(Gly) motifMolecular Biologysensor kinasefumarate030102 biochemistry & molecular biologyChemistryEscherichia coli ProteinsCell MembraneHistidine kinaseGene Expression Regulation BacterialCell BiologyPeriplasmic spacelinkerTransmembrane proteinoxidative Cys cross-linkingTransmembrane domain030104 developmental biologyMembrane proteinProtein kinase domainHelixBiophysicsProtein MultimerizationProtein Kinasestransmembrane signalingLinkerResearch ArticleTM transmembraneJournal of Biological Chemistry
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Hog1p activation by marasmic acid through inhibition of the histidine kinase Sln1p

2016

BACKGROUND The histidine kinase (HK) MoHik1p within the high-osmolarity glycerol (HOG) pathway is known to be the target of the fungicide fludioxonil. Treatment of the fungus with fludioxonil causes an uncontrolled hyperactivation of the pathway and cell death. In this study, we used a target-based in vivo test system with mutant strains of the rice blast fungus Magnaporthe oryzae to search for new fungicidal compounds having various target locations within the HOG pathway. Mutants with inactivated HOG signalling are resistant to fungicides having the target located in the HOG pathway. RESULTS The HK MoSln1p was identified as being involved in the new antifungal mode of action of marasmic a…

0301 basic medicineFungal proteinMagnaporthebiologyMutantHistidine kinaseGeneral MedicineFludioxonilbiology.organism_classificationMicrobiology03 medical and health sciencesMetabolic pathway030104 developmental biologyBiochemistryInsect SciencePhosphorylationMode of actionAgronomy and Crop SciencePest Management Science
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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

2020

13 páginas, 6 figuras, 3 tablas

0301 basic medicineModels MolecularBioquímicaHistidine KinaseProtein ConformationScience030106 microbiologyPhosphataseGeneral Physics and AstronomyMicrobiologiaCrystallography X-RayModels BiologicalBiochemistryMicrobiologyGeneral Biochemistry Genetics and Molecular BiologyCatalysisArticleEnzyme catalysis03 medical and health sciencesResidue (chemistry)Protein structureBacterial ProteinsMultienzyme ComplexesHistidineThermotoga maritimaPhosphorylationlcsh:ScienceAuthor CorrectionHistidineX-ray crystallographyMultidisciplinaryEffectorChemistryEscherichia coli ProteinsQGeneral ChemistryHydrogen-Ion ConcentrationResponse regulator030104 developmental biologyBiochemistryMutationTrans-ActivatorsPhosphorylationlcsh:QBacterial Outer Membrane Proteins
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Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor

2017

Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of t…

0301 basic medicineModels MolecularHistidine Kinase030106 microbiologyMolecular ConformationCitric Acid03 medical and health sciencesStructure-Activity RelationshipBacterial ProteinsPAS domainProtein Interaction Domains and MotifsAmino Acid SequenceHistidineMultidisciplinaryChemistryKinaseHistidine kinaseGeobacillusMembrane ProteinsBiological SciencesTransmembrane proteinCell biologyCytosolHelixSignal transductionProtein BindingSignal Transduction
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Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

2006

SUMMARY Two-component signal-transducing systems are ubiquitously distributed communication interfaces in bacteria. They consist of a histidine kinase that senses a specific environmental stimulus and a cognate response regulator that mediates the cellular response, mostly through differential expression of target genes. Histidine kinases are typically transmembrane proteins harboring at least two domains: an input (or sensor) domain and a cytoplasmic transmitter (or kinase) domain. They can be identified and classified by virtue of their conserved cytoplasmic kinase domains. In contrast, the sensor domains are highly variable, reflecting the plethora of different signals and modes of sens…

0303 health sciencesHistidine Kinase030306 microbiologyKinaseHistidine kinaseReviewsBiologyBacterial Physiological PhenomenaMicrobiologyTwo-component regulatory systemTransmembrane proteinCell biologyHAMP domain03 medical and health sciencesResponse regulatorInfectious DiseasesBacterial ProteinsSignal transductionProtein KinasesMolecular BiologyHistidineSignal Transduction030304 developmental biologyMicrobiology and Molecular Biology Reviews
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Illuminating a Phytochrome Paradigm – a Light-Activated Phosphatase in Two-Component Signaling Uncovered

2020

ABSTRACTBacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome fromDeinococcus radiodurans(DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome fromAgrobacterium fabrum(AgP1). Whereas AgP1 acts as a conventional histidine kinase, we identify DrBp…

0303 health sciencesPhytochromebiologyChemistryKinasePhosphataseHistidine kinaseDeinococcus radioduransbiology.organism_classificationCell biology03 medical and health sciencesResponse regulator0302 clinical medicineKinase activity030217 neurology & neurosurgeryHistidine030304 developmental biology
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Requirement of the Lactobacillus casei MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway.

2009

ABSTRACTLactobacillus caseican metabolizel-malic acid via malolactic enzyme (malolactic fermentation [MLF]) or malic enzyme (ME). Whereas utilization ofl-malic acid via MLF does not support growth, the ME pathway enablesL. caseito grow onl-malic acid. In this work, we have identified in the genomes ofL. caseistrains BL23 and ATCC 334 a cluster consisting of two diverging operons,maePEandmaeKR, encoding a putative malate transporter (maeP), an ME (maeE), and a two-component (TC) system belonging to the citrate family (maeKandmaeR). Homologous clusters were identified inEnterococcus faecalis,Streptococcus agalactiae,Streptococcus pyogenes, andStreptococcus uberis. Our results show that ME is …

DNA BacterialLactobacillus caseiHistidine KinaseMalic enzymeCatabolite repressionDNA FootprintingMalatesGenetics and Molecular Biologymedicine.disease_causeApplied Microbiology and Biotechnologychemistry.chemical_compoundBacterial ProteinsOperonmedicineEnterococcus faecalisDirect repeatPromoter Regions Geneticchemistry.chemical_classificationEcologybiologySequence Homology Amino AcidGene Expression Profilingfungifood and beveragesStreptococcusGene Expression Regulation Bacterialbiology.organism_classificationMolecular biologyAmino acidResponse regulatorLacticaseibacillus caseichemistryBiochemistryMultigene FamilyStreptococcus pyogenesMalic acidProtein KinasesMetabolic Networks and PathwaysFood ScienceBiotechnologyProtein BindingSignal TransductionTranscription FactorsApplied and environmental microbiology
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Phosphorylation and DNA binding of the regulator DcuR of the fumarate-responsive two-component system DcuSR of Escherichia coli

2004

The function of the response regulator DcuR of the DcuSR fumarate two-component sensory system of Escherichia coli was analysed in vitro. Isolated DcuR protein was phosphorylated by the sensory histidine kinase, DcuS, and ATP, or by acetyl phosphate. In gel retardation assays with target promoters (frdA, dcuB, dctA), phosphoryl DcuR (DcuR-P) formed a high-affinity complex, with an apparent K D (app. K D) of 0·2–0·3 μM DcuR-P, and a low-affinity (app. K D 0·8–2 μM) complex. The high-affinity complex was formed only with promoters transcriptionally-regulated by DcuSR, whereas low-affinity binding was seen also with some DcuSR-independent promoters. The binding site of DcuR-P at the dcuB promo…

DNA BacterialTranscription GeneticMolecular Sequence DataBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundFumaratesEscherichia colimedicinePhosphorylationBinding sitePromoter Regions GeneticEscherichia coliBinding SitesBase SequenceEscherichia coli ProteinsHistidine kinasePromoterGene Expression Regulation BacterialMolecular biologyTwo-component regulatory systemDNA-Binding ProteinsResponse regulatorchemistryBiochemistryPhosphorylationProtein KinasesDNASignal TransductionTranscription FactorsMicrobiology
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Oligomeric Sensor Kinase DcuS in the Membrane of Escherichia coli and in Proteoliposomes: Chemical Cross-linking and FRET Spectroscopy

2010

The DcuSR (dicarboxylate uptake sensor and regulator) system of Escherichia coli is a typical two-component system consisting of a membranous sensor kinase (DcuS) and a cytoplasmic response regulator (DcuR) (11, 26, 48). DcuS responds to C4-dicarboxylates like fumarate, malate, or succinate (19). In the presence of the C4-dicarboxlates, the expression of the genes of anaerobic fumarate respiration (dcuB, fumB, and frdABCD) and of aerobic C4-dicarboxylate uptake (dctA) is activated. DcuS is a histidine protein kinase composed of two transmembrane helices with an intermittent sensory PAS domain in the periplasm (PASP) that was also termed the PDC domain (for PhoQ/DcuS/DctB/CitA domain or fold…

Escherichia coli ProteinsProteolipidsCell MembraneGreen Fluorescent ProteinsHistidine kinaseAutophosphorylationBiologyMicrobiologyLuminescent ProteinsResponse regulatorTransmembrane domainSpectrometry FluorescenceProtein kinase domainBiochemistryPAS domainEscherichia coliFluorescence Resonance Energy TransferKinase activityProtein kinase AProtein KinasesMolecular BiologySignal TransductionJournal of Bacteriology
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