Study on the photoreaction dynamics of blue light sensor protein YtvA from Bacillus subtilis

点击翻译按钮获取中文摘要

We investigated the photoreaction dynamics of the blue light sensor protein YtvA to elucidate how the light signal is transferred from the LOV domain to the STAS domain using time-resolved transient grating (TG) method. The concentration dependence of the TG signals and cross-linking measurement showed that YtvA is in equilibrium between the hexamer and the dimer in the ground state. The hexamer underwent the global reaction which was manifested as a decrease in D. The D change of the hexamer might be caused by the change in inter-protein interaction between the dimers. Additionally, we have found significant effect of the salt concentration on the equilibrium in the ground state, which might be relevant for its salt stress response.