0000000001000188

AUTHOR

Andreas Möglich

showing 4 related works from this author

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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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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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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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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