Abstract
The LOV domain is a signal transducing component found in a large variety of proteins that is responsible for sensing different stimuli such as light, oxygen and voltage. The LOV protein Vivid regulates blue light responses in the filamentous fungi Neurospora crassa. We have probed light-induced structural transitions in Vivid using laser excitation coupled with time-resolved small angle x-ray scattering. We observe conformationally distinct monomer states of Vivid that differentially participate in light-induced dimerization. These measurements allow us to propose a mechanism for how light regulates the oligomeric states of LOV domains.
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