Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy

Tryptophan residues at the dimer interface of the plant photoreceptor UVR8 promote monomerisation after UV-B absorption via a so far unknown mechanism. Using FTIR spectroscopy we assign light-induced structural transitions of UVR8 mainly to amino acid side chains without major transformations of the...

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Bibliographic Details
Published in:Photochemical & photobiological sciences 2015-02, Vol.14 (2), p.252-257
Main Authors: Heilmann, Monika, Christie, John M., Kennis, John T. M., Jenkins, Gareth I., Mathes, Tilo
Format: Article
Language:English
Subjects:
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - genetics
Biochemistry
Biomaterials
Chemistry
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - genetics
Light
Mutation
Photochemical Processes
Physical Chemistry
Plant Sciences
Protein Conformation - radiation effects
Spectrometry, Fluorescence
Spectroscopy, Fourier Transform Infrared
Tryptophan - chemistry
Tryptophan - genetics
Vibration
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Summary:Tryptophan residues at the dimer interface of the plant photoreceptor UVR8 promote monomerisation after UV-B absorption via a so far unknown mechanism. Using FTIR spectroscopy we assign light-induced structural transitions of UVR8 mainly to amino acid side chains without major transformations of the secondary structure of the physiologically relevant C-terminal extension. Additionally, we assign the monomerisation associated increase and red shift of the UVR8 tryptophan emission to a photoinduced rearrangement of tryptophan side chains and a relocation of the aspartic acid residues D96 and D107, respectively. By illumination dependent emission spectroscopy we furthermore determined the quantum yield of photoinduced monomerisation to 20 ± 8%.
ISSN:1474-905X
1474-9092
DOI:10.1039/c4pp00246f