Search results for "Deinococcus"

showing 10 items of 30 documents

Modulation of Structural Heterogeneity Controls Phytochrome Photoswitching

2019

Phytochromes sense red/far-red light and control many biological processes in plants, fungi, and bacteria. Although crystal structures of dark and light adapted states have been determined, the molecular mechanisms underlying photoactivation remains elusive. Here we demonstrate that the conserved tongue region of the PHY domain of a 57kDa photosensory module of Deinococcus radiodurans phytochrome, changes from a structurally heterogeneous dark state to an ordered light activated state. The results were obtained in solution by utilizing a laser-triggered activation approach detected on the atomic level with high-resolution protein NMR spectroscopy. The data suggest that photosignaling of phy…

Models MolecularLightTongue regionBiophysicsphototransduction03 medical and health sciences0302 clinical medicineProtein DomainsPHYmolekyylidynamiikkaprotein structureNMR-spektroskopiaNuclear Magnetic Resonance Biomolecular030304 developmental biologyphytochrome0303 health sciencesPhytochromebiologyChemistryProtein NMR SpectroscopyDeinococcus radioduransArticlesDarknessbiology.organism_classificationmolecular dynamicsNMRStructural heterogeneityDark stateModulationBiophysicsvalokemiaproteiinitDeinococcusPhytochrome030217 neurology & neurosurgeryBiophysical Journal
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The hairpin extension controls solvent access to the chromophore binding pocket in a bacterial phytochrome: a UV-vis absorption spectroscopy study.

2021

AbstractSolvent access to the protein interior plays an important role in the function of many proteins. Phytochromes contain a specific structural feature, a hairpin extension that appears to relay structural information from the chromophore to the rest of the protein. The extension interacts with amino acids near the chromophore, and hence shields the chromophore from the surrounding solvent. We envision that the detachment of the extension from the protein surface allows solvent exchange reactions in the vicinity of the chromophore. This can facilitate for example, proton transfer processes between solvent and the protein interior. To test this hypothesis, the kinetics of the protonation…

Models MolecularProtein ConformationProtonation010402 general chemistryPhotochemistry01 natural sciencespH jump03 medical and health scienceschemistry.chemical_compoundPhytochrome ADeprotonationBacterial ProteinsPhotostationary statePhysical and Theoretical Chemistrychromophore protein systems030304 developmental biology0303 health sciencesBiliverdinBinding SitesPhytochromeProtein dynamicsBiliverdineconformational substatesChromophoreHydrogen-Ion Concentrationsolvent gating0104 chemical sciencesKineticschemistryprotein dynamicsSolventsSpectrophotometry UltravioletproteiinitvalokemiaDeinococcusPhytochromeProtonsPhotochemicalphotobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
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Fluorescence Properties of the Chromophore-Binding Domain of Bacteriophytochrome from Deinococcus radiodurans

2013

Fluorescent proteins are versatile tools for molecular imaging. In this study, we report a detailed analysis of the absorption and fluorescence properties of the chromophore-binding domain from Deinococcus radiodurans and its D207H mutant. Using single photon counting and transient absorption techniques, the average excited state lifetime of both studied systems was about 370 ps. The D207H mutation slightly changed the excited state decay profile but did not have a considerable effect on the average decay time of the system or the shape of the absorption and emission spectra of the biliverdin chromophore. We confirmed that the fluorescence properties of both samples are very similar in vivo…

Time FactorsFluorescence in the life sciencesPhotochemistrychemistry.chemical_compoundBimolecular fluorescence complementationBacterial ProteinsEscherichia coliMaterials ChemistryPhysical and Theoretical Chemistryta116BiliverdinbiologyPhytochromeBiliverdineta1182Deinococcus radioduransChromophorebiology.organism_classificationFluorescenceRecombinant ProteinsProtein Structure TertiarySurfaces Coatings and FilmschemistryMutationQuantum TheorySpectrophotometry UltravioletDeinococcusBinding domainThe Journal of Physical Chemistry B
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Extremophilic taxa predominate in a microbial community of photovoltaic panels in a tropical region

2021

ABSTRACT Photovoltaic panels can be colonized by a highly diverse microbial diversity, despite life-threatening conditions. Although they are distributed worldwide, the microorganisms living on their surfaces have never been profiled in tropical regions using 16S rRNA high-throughput sequencing and PICRUst metagenome prediction of functional content. In this work, we investigated photovoltaic panels from two cities in southeast Brazil, Sorocaba and Itatiba, using these bioinformatics approach. Results showed that, despite significant differences in microbial diversity (p < 0.001), the taxonomic profile was very similar for both photovoltaic panels, dominated mainly by Proteobacteria,…

Tropical Climatefood.ingredientbiologyConstruction MaterialsEcologyPhylumMicrobiotaCyanobacteriabiology.organism_classificationSphingomonasMicrobiologyExtremophilesfoodMicrobial population biologyMetagenomicsGenusRNA Ribosomal 16SHymenobacterSolar EnergyGeneticsMetagenomeDeinococcusProteobacteriaMolecular BiologyFEMS Microbiology Letters
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Connection between Absorption Properties and Conformational Changes in Deinococcus radiodurans Phytochrome

2014

Phytochromes consist of several protein domains and a linear tetrapyrrole molecule, which interact as a red-light-sensing system. In this study, size-exclusion chromatography and light-scattering techniques are combined with UV-vis spectroscopy to investigate light-induced changes in dimeric Deinococcus radiodurans bacterial phytochrome (DrBphP) and its subdomains. The photosensory unit (DrCBD-PHY) shows an unusually stable Pfr state with minimal dark reversion, whereas the histidine kinase (HK) domain facilitates dark reversion to the resting state. Size-exclusion chromatography reveals that all phytochrome fragments remain as dimers in the illuminated state and dark state. Still, the elut…

biologyPhytochromeProtein ConformationElutionProtein domainHistidine kinaseta1182Deinococcus radioduransSDG 10 - Reduced Inequalitiesbiology.organism_classificationBiochemistryTetrapyrroleProtein Structure Tertiarychemistry.chemical_compoundDark stateBacterial ProteinsBiochemistrychemistry/dk/atira/pure/sustainabledevelopmentgoals/reduced_inequalitiesBiophysicsMoleculeSpectrophotometry UltravioletDeinococcusPhytochromeBiochemistry
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ERA-experiment “space biochemistry”

1995

Abstract The general goal of the experiment was to study the response of anhydrobiotic (metabolically dormant) microorganisms (spores of Bacillus subtilis, cells of Deinococcus radiodurans, conidia of Aspergillus species) and cellular constituents (plasmid DNA, proteins, purple membranes, amino acids, urea) to the extremely dehydrating conditions of open space, in some cases in combination with irradiation by solar UV-light. Methods of investigation included viability tests, analysis of DNA damages (strand breaks, DNA-protein cross-links) and analysis of chemical effects by spectroscopic, electrophoretic and chromatographic methods. The decrease in viability of the microorganisms was as exp…

chemistry.chemical_classificationAtmospheric SciencebiologyDNA damageChemistryMicroorganismFungal geneticsAerospace EngineeringAstronomy and AstrophysicsDeinococcus radioduransBacillus subtilisbiology.organism_classificationAmino acidchemistry.chemical_compoundGeophysicsBiochemistrySpace and Planetary ScienceUreaGeneral Earth and Planetary SciencesDNAAdvances in Space Research
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Removal of Chromophore-proximal Polar Atoms Decreases Water Content and Increases Fluorescence in a Near Infrared Phytofluor

2015

Genetically encoded fluorescent markers have revolutionized cell and molecular biology due to their biological compatibility, controllable spatiotemporal expression, and photostability. To achieve in vivo imaging in whole animals, longer excitation wavelength probes are needed due to the superior ability of near infrared light to penetrate tissues unimpeded by absorbance from biomolecules or autofluorescence of water. Derived from near infrared-absorbing bacteriophytochromes, phytofluors are engineered to fluoresce in this region of the electromagnetic spectrum, although high quantum yield remains an elusive goal. An invariant aspartate residue is of utmost importance for photoconversion in…

chromophore binding domain (CBD)Analytical chemistryQuantum yieldPhotochemistryBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryFluorescence spectroscopychemistry.chemical_compoundDeinococcus radioduransWiPhy2Side chainMolecular Biologylcsh:QH301-705.5Wisconsin infrared phytofluor (WiPhy2)Original ResearchBiliverdinta114Physicsta1182Excitation-emission matrix (EEM)ChromophorePhotobleachingFluorescenceexcitation-emission matrix (EEM)chemistrylcsh:Biology (General)Excited statetetrapyrroleFrontiers in Molecular Biosciences
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The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography

2016

Scientific reports 6, 35279 (2016). doi:10.1038/srep35279

crystal structure000Protein ConformationREARRANGEMENTSTemperaturePROTEINCrystallography X-RayphytochromeskidetiedeTRANSDUCTIONArticleX-RAY-DIFFRACTIONCHROMOPHORE-BINDING DOMAINGROUND-STATEddc:000RED LIGHT3111 BiomedicineDeinococcusPhytochromesense organsBACTERIOPHYTOCHROMEFLUORESCENCEroom temperatureCrystallizationPHOTOCONVERSION
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Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome

2022

Funding Information: This work was supported by Academy of Finland grants 285461 (H.T.), 330678 (H.T., J.R.), 277194 (H.L.), and 290677 (S.M.). We acknowledge the European Synchrotron Radiation Facility (ESRF) for providing synchrotron access for crystal data collection. We thank Prof. Janne Ihalainen (University of Jyväskylä) for all the help in all aspects of the paper, Prof. Gerrit Groenhof (University of Jyväskylä) for support, and Prof. Nikolai V. Tkachenko (Tampere University) for help and facilities for time-resolved absorption spectroscopy. We also thank M.Sc. Alli Liukkonen (University of Jyväskylä) and Dr. Heikki Häkkänen (University of Jyväskylä) for the assistance in laboratory …

fytokromitphytochrome structureProtein ConformationPhytochrome structureSpectral responsesspektroskopiafotobiologiabakteeritBacterial ProteinsHistidinePhysical and Theoretical ChemistryBinding Sites221 Nanotechnologyspectral responsesWaterBiliverdin protonationsäteilyWater networkkidetiedewater networkTyrosine1182 Biochemistry cell and molecular biologyPhytochromeDeinococcusproteiinitvalokemiabiliverdin protonationvalo
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Photoinduced changes in phytochromes studied by means of low temperature UV-Vis spectroscopy

2018

Phytochromes are a major family of red-light-sensing kinases that control diverse cellular functions in plants, bacteria and fungi. These proteins must relay structural signals from the sensory site over large distances to regulatory output domains. To accomplish this function, they undergo rather large structural changes from one state to another. The general aim of this work was to study these structural changes and possible protonation states of the photosensory core of the bacteriophytochrome from Deinococcus radiodurans in the intermediate states of the photoreaction, which became possible to observe under low temperatures. Moreover, it was interesting to investigate the role Serine272…

phytochromeDeinococcus radioduransintermediateslow temperature UV-Vis spectroscopyphotocycle
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