Search results for "HISTIDINE KINASES"

showing 5 items of 5 documents

Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

2021

Bacterial 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 from Deinococcus 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 from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP a…

Histidine KinaseLightPROTEINSScienceAgrobacteriumHISTIDINE KINASESKinasesMolecular Dynamics SimulationPhotoreceptors MicrobialTRANSDUCTIONArticleCYANOBACTERIAL PHYTOCHROME CPH1ACTIVATIONBacterial ProteinsProtein DomainsCRYSTAL-STRUCTUREPHOSPHORYLATIONX-ray crystallographyBacterial structural biologyQREARRANGEMENTSphotoreceptorsAGROBACTERIUM-TUMEFACIENSPhosphoric Monoester HydrolasesINSIGHTSbacterial phytochromesEnzyme mechanismsbacteriaDeinococcus3111 BiomedicineSignal Transduction
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Optogenetic Control of Bacterial Expression by Red Light

2022

In optogenetics, as in nature, sensory photoreceptors serve to control cellular processes by light. Bacteriophytochrome (BphP) photoreceptors sense red and far-red light via a biliverdin chromophore and, in response, cycle between the spectroscopically, structurally, and functionally distinct Pr and Pfr states. BphPs commonly belong to two-component systems that control the phosphorylation of cognate response regulators and downstream gene expression through histidine kinase modules. We recently demonstrated that the paradigm BphP from Deinococcus radiodurans exclusively acts as a phosphatase but that its photosensory module can control the histidine kinase activity of homologous receptors.…

HistoryfytokromitSIGNALING MECHANISMHistidine KinaseLightPolymers and PlasticsBiomedical EngineeringHISTIDINE KINASESfotobiologiasensory photoreceptorBiochemistry Genetics and Molecular Biology (miscellaneous)Industrial and Manufacturing EngineeringbakteeritOPTICAL CONTROLgeeniekspressioBusiness and International ManagementoptogeneticsHEME OXYGENASEGENE-EXPRESSIONphytochromeoptogenetiikkaPHOTORECEPTORSBacteriaBiliverdineREARRANGEMENTSBACTERIOPHYTOCHROMESGeneral MedicinePhosphoric Monoester HydrolasesOptogeneticsreseptorit (biokemia)two-component systemESCHERICHIA-COLIgene expression1182 Biochemistry cell and molecular biology3111 BiomedicinePhytochromevalosignal transductionSSRN Electronic Journal
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Evidence of a New MoYpd1p Phosphotransferase Isoform in the Multistep Phosphorelay System of Magnaporthe oryzae

2021

Different external stimuli are perceived by multiple sensor histidine kinases and transmitted by phosphorylation via the phosphotransfer protein Ypd1p in the multistep phosphorelay system of the high osmolarity glycerol signaling pathway of filamentous fungi. How the signal propagation takes place is still not known in detail since multiple sensor histidine kinase genes in most filamentous fungi are coded in the genome, whereas only one gene for Ypd1p exists. That raises the hypothesis that various Ypd1p isoforms are produced from a single gene sequence, perhaps by alternative splicing, facilitating a higher variability in signal transduction. We found that the mRNA of MoYPD1 in the rice bl…

Microbiology (medical)Gene isoformQH301-705.5MutantPlant ScienceBiology<i>Magnaporthe oryzae</i>Phosphotransferasealternative splicingphosphotransferComplementary DNAanatomy_morphologyBiology (General)GeneEcology Evolution Behavior and SystematicsCommunicationAlternative splicingHistidine kinasephosphorelayhigh osmolarity glycerol (HOG) pathwayMagnaporthe oryzaeCell biologyProteomehistidine kinasesYPD1signalingsignal transductionJournal of Fungi
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Tips and turns of bacteriophytochrome photoactivation

2020

Phytochromes are ubiquitous photosensor proteins, which control the growth, reproduction and movement in plants, fungi and bacteria. Phytochromes switch between two photophysical states depending on the light conditions. In analogy to molecular machines, light absorption induces a series of structural changes that are transduced from the bilin chromophore, through the protein, and to the output domains. Recent progress towards understanding this structural mechanism of signal transduction has been manifold. We describe this progress with a focus on bacteriophytochromes. We describe the mechanism along three structural tiers, which are the chromophore-binding pocket, the photosensory module,…

Models MolecularProtein Conformation116 Chemical sciencesHISTIDINE KINASESSIGNAL-TRANSDUCTIONfotobiologiabacteriophytochrome photoactivation010402 general chemistry01 natural sciencesbakteeritPhytochrome B03 medical and health sciencesProtein structureBacterial ProteinsINDUCED PROTON RELEASEPHYTOCHROME-BCRYSTAL-STRUCTUREPhysical and Theoretical Chemistry030304 developmental biologyINDUCED CONFORMATIONAL-CHANGESPhysics0303 health sciencesRESONANCE RAMANMechanism (biology)AGROBACTERIUM-TUMEFACIENSPhotochemical ProcessesMolecular machine0104 chemical sciencesINFRARED FLUORESCENT PROTEINSCHROMOPHORE-BINDING DOMAINBiophysics1182 Biochemistry cell and molecular biologyvalokemiaproteiinitPhytochromeSignal TransductionPhotochemical &amp; Photobiological Sciences
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Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

2017

Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a t…

Models MolecularkinaasitentsyymitHistidine KinaseLightProtein ConformationScienceQCrystallography X-RayArticleProtein Structure SecondaryaktivointiBacterial ProteinsProtein DomainsX-Ray DiffractionphotoactivationScattering Small AngleNanotechnologysensor histidine kinasesNature Communications
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