Search results for "PHOTOCONVERSION"

showing 5 items of 5 documents

On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome

2018

Phytochromes are photoreceptors in plants, fungi, and various microorganisms and cycle between metastable red light-absorbing (Pr) and far-red light-absorbing (Pfr) states. Their light responses are thought to follow a conserved structural mechanism that is triggered by isomerization of the chromophore. Downstream structural changes involve refolding of the so-called tongue extension of the phytochrome-specific GAF-related (PHY) domain of the photoreceptor. The tongue is connected to the chromophore by conserved DIP and PRXSF motifs and a conserved tyrosine, but the role of these residues in signal transduction is not clear. Here, we examine the tongue interactions and their interplay with …

0301 basic medicineModels MolecularCrystallography X-RayBiochemistrybakteeritProtein structurephotoconversionchromophore-binding domainTransferasestructural biologyCRYSTAL-STRUCTURETyrosineDEINOCOCCUS-RADIODURANSbiologyPhytochromeChemistryREARRANGEMENTSProtein Structure and FoldingDeinococcusmutagenesisBinding domainSignal TransductionMODULEPLANT PHYTOCHROMEPhenylalaninefotobiologia03 medical and health sciencesBacterial Proteinsprotein conformationcell signalingprotein structureBACTERIOPHYTOCHROMEMolecular BiologyX-ray crystallographysoluviestintäphytochromeAGP1BINDING DOMAINBinding Sitesta114030102 biochemistry & molecular biologyta1182Deinococcus radioduransCell BiologyChromophorebiology.organism_classificationphotoreceptor030104 developmental biologyStructural biologyFTIRBiophysicsTyrosineproteiinit3111 Biomedicineröntgenkristallografia
researchProduct

Localization microscopy of DNA in situ using Vybrant(®) DyeCycle™ Violet fluorescent probe: A new approach to study nuclear nanostructure at single m…

2016

Higher order chromatin structure is not only required to compact and spatially arrange long chromatids within a nucleus, but have also important functional roles, including control of gene expression and DNA processing. However, studies of chromatin nanostructures cannot be performed using conventional widefield and confocal microscopy because of the limited optical resolution. Various methods of superresolution microscopy have been described to overcome this difficulty, like structured illumination and single molecule localization microscopy. We report here that the standard DNA dye Vybrant(®) DyeCycle™ Violet can be used to provide single molecule localization microscopy (SMLM) images of …

0301 basic medicine02 engineering and technologyBiologyChromosomeslaw.inventionVybrant DyeCycle Violet03 medical and health sciencesDNA dyesHigher Order Chromatin StructureConfocal microscopylawphotoconversionMicroscopyChlorocebus aethiopsAnimalsdSTORMSMLMVero CellsFluorescent Dyeschromatin structureCell NucleusResolution (electron density)DNA replicationCell BiologyDNA021001 nanoscience & nanotechnologySingle Molecule ImagingFluorescenceSingle Molecule ImagingChromatinCell biologyNanostructures030104 developmental biologyDrosophila melanogasterMicroscopy FluorescenceBiophysics0210 nano-technologyExperimental cell research
researchProduct

Single molecule localization microscopy of the distribution of chromatin using Hoechst and DAPI fluorescent probes.

2014

Several approaches have been described to fluorescently label and image DNA and chromatin in situ on the single-molecule level. These superresolution microscopy techniques are based on detecting optically isolated, fluorescently tagged anti-histone antibodies, fluorescently labeled DNA precursor analogs, or fluorescent dyes bound to DNA. Presently they suffer from various drawbacks such as low labeling efficiency or interference with DNA structure. In this report, we demonstrate that DNA minor groove binding dyes, such as Hoechst 33258, Hoechst 33342, and DAPI, can be effectively employed in single molecule localization microscopy (SMLM) with high optical and structural resolution. Upon ill…

DNA ReplicationHoechstDNA RepairDNA repairBiologyfluorescence microscopyDAPIchemistry.chemical_compoundphotoconversionsuper-resolution microscopylocalization microscopyFluorescence microscopeSPDMAnimalsHumansDAPIdSTORMSMLMFluorescent DyesMicroscopySuper-resolution microscopynucleusDNA replicationdSTORCell BiologyDNADNA Minor Groove BindingChromatinChromatinCell biologychemistryMicroscopy FluorescencechromatinblinkingDNAResearch PaperNucleus (Austin, Tex.)
researchProduct

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
researchProduct

Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome

2018

Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxobacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this ph…

MODULE0301 basic medicinePHOTOACTIVE YELLOW PROTEINSIGNALING MECHANISMabsorption spectraMutantfotobiologiaphytochromesBiochemistryyhteyttäminenbakteeritSTIGMATELLA-AURANTIACA03 medical and health sciencesFRUITING BODY FORMATIONGeneral Materials ScienceMolecular replacementStigmatella aurantiacalcsh:ScienceUNUSUAL BACTERIOPHYTOCHROMEPHOTOCONVERSIONHistidine030102 biochemistry & molecular biologybiologyPhytochromeChemistryCRYSTALLOGRAPHYta1182photosynthetic bacteriaphotoreceptorsGeneral ChemistryChromophoreCondensed Matter Physicsbiology.organism_classification030104 developmental biologyCHROMOPHORE-BINDING DOMAINBiophysicsmyxobacterialcsh:Q3111 BiomedicinePhotosynthetic bacteriaproteiinitMOLECULAR REPLACEMENTBinding domainIUCrJ
researchProduct