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Plant and Cell Physiology Advance Access published online on October 4, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci208
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received August 9, 2005
Accepted September 27, 2005

Rapid Paper

Tryptophan at Position 104 Is Involved in Transforming Light Signal into Changes of {beta}-Sheet Structure for the Signaling State in the BLUF Domain of AppA

Shinji Masuda 1* 3, Koji Hasegawa 2 3, and Taka-aki Ono 2

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

* To whom correspondence should be addressed.
Shinji Masuda, E-mail: shmasuda{at}bio.titech.ac.jp


  Abstract

AppA is a member of a flavin adenine dinucleotide (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 apoprotein had been selectively labeled with 13C. The light-induced FTIR spectrum of the W104A mutant AppA126 revealed bands corresponding to a C(4)=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 1632(+)/1619(-) cm-1 caused by changes in the {beta}-sheet structure were eliminated by the mutation, indicating that Trp104 is responsible for transforming the light signal into a specific {beta}-sheet structure change in the apoprotein of AppA BLUF domain in the signaling state.

Keywords: AppA; Blue light receptor; BLUF; Flavin; FTIR; Signaling transduction.

3 S.M. and K.H. contributed equally to this work.


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