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• W2282914127 abstract "Phytochromes are red-light sensing proteins of bacteria, algae, plants, and fungi. A central feature of the function of phytochromes is a light-induced conversion between a red absorbing (Pr) state and a far-red absorbing state (Pfr). The photosensory unit (CBD-PHY) of Deinococcus radiodurans bacteriophytochrome is a dimeric protein consisting of a C-terminal chromophore binding (CBD) domain and a phytochromeassociated (PHY) domain. Recent crystal and solution structures of CBD-PHY have shown that the separation between the two PHY domains increases when the protein is converted from Pr to Pfr state as a result of red-light absorption. Forster resonance energy transfer (FRET) based measurements were designed in this work to be used as an alternative, non-invasive, and cost-efficient way for probing the PHY domain separation in Pr and Pfr. CBDPHY engineered with cysteine insertions at the ends of the PHY domains (E373/CC/G374) and one surface cysteine substituted with serine (C93S) was expressed in E. coli strain BL21 (DE3) cells and purified with high-pressure liquid chromatography. A maleimide-based labeling scheme was developed for attaching a FRET donor (D) – acceptor (A) pair (Alexa Fluor 488 – Alexa Fluor 546) to the cysteine insertions. Steadystate fluorescence emission spectra, fluorescence decays, and steady-state and time-resolved fluorescence anisotropies were measured for determining FRET efficiencies and corresponding D-A distances in Pr and Pfr. Emission spectrum of DA-labeled CBD-PHY in Pr and Pfr revealed FRET-associated intensity changes in both D and A emission. Surprisingly, FRET signal was absent from time-resolved results. Furthermore, none of the measurement techniques revealed a difference between Pr and Pfr, and there was discrepancy between D-A distances determined from steady-state results and those evaluated from earlier solution structures. Multiple explanations can be proposed for the unexpected results. It is evident that further development of protein labeling protocols is still needed. There is also a possibility that the system is more complicated than what was initially expected because of processes such as quenching of the dyes or FRET between the dyes and biliverdin molecules bound to the CBD-domains." @default.
• W2282914127 created "2016-06-24" @default.
• W2282914127 creator A5024164189 @default.
• W2282914127 date "2016-01-01" @default.
• W2282914127 modified "2023-09-27" @default.
• W2282914127 title "Fluorescence labeling of the photosensory unit of Deinococcus radiodurans bacteriophytochrome for Förster resonance energy transfer studies" @default.
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