Structural insights into photoactivation of plant Cryptochrome-2
| Autor: | Samuel L. Deck, Malathy Palayam, Angelica M. Guercio, Nitzan Shabek, Lior Tal, Jagadeesan Ganapathy |
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| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
Protein Structure QH301-705.5 Circadian clock Arabidopsis Medicine (miscellaneous) CRYPTOCHROME 2 Flowering time 01 natural sciences Article General Biochemistry Genetics and Molecular Biology Quaternary 03 medical and health sciences chemistry.chemical_compound Cryptochrome Light responses Active state Amino Acid Sequence Biology (General) Protein Structure Quaternary X-ray crystallography 030304 developmental biology Flavin adenine dinucleotide 0303 health sciences biology Arabidopsis Proteins Chromophore biology.organism_classification Cryptochromes chemistry Structural biology Biophysics Flavin-Adenine Dinucleotide sense organs General Agricultural and Biological Sciences 010606 plant biology & botany |
| Zdroj: | Communications biology, vol 4, iss 1 Communications Biology, Vol 4, Iss 1, Pp 1-11 (2021) Communications Biology |
| Popis: | Cryptochromes (CRYs) are evolutionarily conserved photoreceptors that mediate various light-induced responses in bacteria, plants, and animals. Plant cryptochromes govern a variety of critical growth and developmental processes including seed germination, flowering time and entrainment of the circadian clock. CRY’s photocycle involves reduction of their flavin adenine dinucleotide (FAD)-bound chromophore, which is completely oxidized in the dark and semi to fully reduced in the light signaling-active state. Despite the progress in characterizing cryptochromes, important aspects of their photochemistry, regulation, and light-induced structural changes remain to be addressed. In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state. Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate distinct structural elements and critical residues that dynamically partake in photo-induced oligomerization. Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins. Palayam, Ganapathy, Guercio et al. determine the crystal structure of the photosensory domain of Arabidopsis Cryptochrome-2 (CRY2) in a tetrameric active state, identifying critical residues that participate in photo-induced oligomerization of CRY2. This study offers an updated model of CRY’s photoactivation mechanism. |
| Databáze: | OpenAIRE |
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