Structure determination and domain interaction of the photochromic protein YtvA from Bacillus subtilis

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Light is an important stimulus for plants and various bacteria. These organisms have therefore developed a number of photoreceptors, usually consisting of a protein and an organic cofactor, to sense light of different wavelengths. The detailed mechanism of light perception, i.e., the “primary event” and the consecutively following conformational changes of the receptor, are still only poorly understood. In this project the structure and domain interaction of the flavin-binding, blue-light photoceptor YtvA from Bacillus subtilis will be studied. This photoreceptor is a two-domain protein, consisting of a LOV (light, oxygen, voltage) domain (harboring a flavin chromophore) and a STAS (Sulphate Transporters AntiSigma-factor antagonist) domain. Utilizing modern NMR-techniques in conjunction with isotopelabeling, the three-dimensional structure of YtvA (which is not yet available) will be determined and the interactions between both domains will be identified. Thus the changes that occur during the transition from the dark into the illuminated (signaling) state as the initial process of signal transduction in biology will be revealed.