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| - Light Induced Structural Changes of a Full-length Protein and Its BLUF Domain inYcgF(Blrp), a Blue-Light Sensing Protein That Uses FAD (BLUF)
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| - Blue-light sensing proteins that use FAD (BLUF) are members of a blue-light receptor familythat is widely distributed among microorganisms. The Escherichia coli YcgF protein is a BLUF proteinconsisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain. TheEAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity. Light-inducedstructural changes for the signaling state formation were studied using the light-induced Fourier transforminfrared (FTIR) difference spectroscopy of both the full-length YcgF protein (YcgF-Full) and its BLUFdomain (YcgF-BLUF). YcgF-Full and YcgF-BLUF showed identical UV−visible absorption spectra offlavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed tothe dark state showing identical kinetics. The light-induced FTIR difference spectrum of YcgF-Full,however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most ofthe IR bands that were induced in the YcgF-Full spectrum. These bands were assigned to the light-induced structural changes of the protein. However, the bands for the C4O stretching of a FADisoalloxazine ring were induced at the same frequency with the same band intensity in the spectra forYcgF-Full and YcgF-BLUF. Furthermore, the YcgF-Full spectrum resembled that of the YcgF-BLUFwhen illuminated at medium-low temperatures because of the selective suppression of protein bands. Thepossibility that full-length-specific protein bands are predominantly ascribed to structural changes of theC-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminalBLUF domain is discussed.
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