Plant and Cell Physiology Advance Access originally published online on October 4, 2005
Plant and Cell Physiology 2005 46(12):1894-1901; doi:10.1093/pcp/pci208
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Tryptophan at Position 104 is Involved in Transforming Light Signal into Changes of ß-sheet Structure for the Signaling State in the BLUF Domain of AppA
1 Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-5801 Japan
2 Laboratory for Photobiology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519–1399, Aoba, Sendai, 980-0845 Japan
* Corresponding authors: Shinji Masuda, E-mail, shmasuda{at}bio.titech.ac.jp; Fax, +81-45-924-5823; Taka-aki Ono, E-mail, takaaki{at}riken.jp;Fax, +81-48-462-4679.
AppA is a member of an FAD-based new class blue-light sensory protein known as sensor of blue light using FAD (BLUF) protein. The spectroscopic properties of an AppA BLUF domain (AppA126), in which the tryptophan residue at position 104 had been replaced with alanine (W104A), were characterized. The W104A mutant AppA126 showed a nearly normal absorption red shift in the FAD UV-visible absorption upon illumination; however, the light state relaxed to the dark state at a rate approximately 150 times faster than that of wild-type AppA126. Light-induced structural changes of FAD and apoprotein in the wild-type and mutant AppA126 were studied by means of light-induced Fourier transform infrared (FTIR) difference spectroscopy using AppA126, in which the apoprotein had been selectively labeled with 13C. The light-induced FTIR spectrum of the W104A mutant AppA126 revealed bands corresponding to a C4 = O stretch of the FAD isoalloxazine ring and structural changes of apoprotein, but with some alterations in the bands’ features. Notably, however, prominent protein bands at 1,632(+)/1,619(–) cm–1 caused by changes in the ß-sheet structure were eliminated by the mutation, indicating that Trp104 is responsible for transforming the light signal into a specific ß-sheet structure change in the apoprotein of the AppA BLUF domain in the signaling state.
3 S.M. and K.H. contributed equally to this work.
4 Present address: Molecular Membrane Biology Laboratory, RIKEN, Wako, 351-0198, Japan.
(Received August 9, 2005; Accepted September 27, 2005)
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