Document Detail


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.
MedLine Citation:
PMID:  16204305     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 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 the AppA BLUF domain in the signaling state.
Authors:
Shinji Masuda; Koji Hasegawa; Taka-aki Ono
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-10-04
Journal Detail:
Title:  Plant & cell physiology     Volume:  46     ISSN:  0032-0781     ISO Abbreviation:  Plant Cell Physiol.     Publication Date:  2005 Dec 
Date Detail:
Created Date:  2005-12-29     Completed Date:  2006-02-28     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9430925     Medline TA:  Plant Cell Physiol     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1894-901     Citation Subset:  IM    
Affiliation:
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-5801 Japan. shmasuda@bio.titech.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Alanine / analysis
Apoproteins / chemistry,  genetics,  physiology
Bacterial Proteins / chemistry*,  genetics,  physiology*
Escherichia coli
Flavoproteins / chemistry*,  genetics,  physiology*
Light*
Light Signal Transduction / physiology*
Mutation
Protein Structure, Secondary
Protein Structure, Tertiary*
Spectroscopy, Fourier Transform Infrared
Time Factors
Tryptophan / analysis*,  physiology*
Ultraviolet Rays
Chemical
Reg. No./Substance:
0/Apoproteins; 0/AppA protein, Rhodobacter sphaeroides; 0/Bacterial Proteins; 0/Flavoproteins; 56-41-7/Alanine; 73-22-3/Tryptophan

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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