Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
Autor: | Yumiko Adachi, Hiroto Nakajima, Itsuki Kobayashi, Osamu Hisatomi |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
chemistry.chemical_classification Conformational change Multidisciplinary 030102 biochemistry & molecular biology Zipper Effector Science Beta sheet Biophysics bZIP domain Molecular biophysics Article Amino acid 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Helix Medicine DNA |
Zdroj: | Scientific Reports Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021) |
ISSN: | 2045-2322 |
Popis: | Light-Oxygen-Voltage (LOV) domains are responsible for detecting blue light (BL) and regulating the activities of effector domains in various organisms. Photozipper (PZ), an N-terminally truncated aureochrome-1 protein, contains a LOV domain and a basic leucin zipper (bZIP) domain and plays a role as a light-activatable transcription factor. PZ is monomeric in the dark state and undergoes non-covalent dimerization upon illumination with BL, subsequently increasing its affinity for the target DNA. To clarify the molecular mechanism of aureochromes, we prepared site-directed mutants of PZ and performed quantitative analyses in the dark and light states. Although the amino acid substitutions in the hinge region between the LOV core and A’α helix had minor effects on the dimerization and DNA-binding properties of PZ, the substitutions in the β-sheet region of the LOV core and in the A’α helix significantly affected these properties. We found that light signals are transmitted from the LOV core to the effector bZIP domain via the hydrophobic residues on the β-sheet. The light-induced conformational change possibly deforms the hydrophobic regions of the LOV core and induces the detachment of the A’α helix to expose the dimerization surface, likely activating the bZIP domain in a light-dependent manner. |
Databáze: | OpenAIRE |
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