0000000001261498

AUTHOR

Henrik Hammaren

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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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