Light-state solution structure of the photocontrolled DNA-binding protein EL222
The transcription factor EL222 regulates gene expression in a light-dependent manner and, as a consequence, has found widespread use in optogenetic applications. At the molecular level, the protein displays a simple architecture consisting of a flavin binding light-oxygen-voltage (LOV) domain and a helix-turn-helix (HTH) DNA binding domain. The crystal structure of dark-state EL222 shows that LOV and HTH domains are tightly packed against each other thereby blocking the recognition of DNA. Upon excitation of the flavin moiety with blue light, EL222 undergoes quick conformational changes that lead to protein dimerization and DNA complexation. However, our knowledge of the light-adapted states remains incomplete. We propose to employ small-angle scattering techniques, SAXS and SANS, in order to model the structural ensembles of EL222 in solution. Specifically, light-activated EL222 will be measured both alone and bound to DNA. The gathered information is expected to shed light on the activation mechanism of LOV photoreceptors and might help in the design of new variants of EL222 with altered optogenetic features.
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Gustavo Fuertes; CHAUDHARI Aditya and MARTEL Anne. (2019). Light-state solution structure of the photocontrolled DNA-binding protein EL222. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-967
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