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Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy

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Abstract

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%.

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Authors and Affiliations

  1. Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, Bower Building, University of Glasgow, Glasgow, G12 8QQ, UK

    Monika Heilmann, John M. Christie & Gareth I. Jenkins

  2. Biophysics Group, Department of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands

    John T. M. Kennis & Tilo Mathes

Authors
  1. Monika Heilmann
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  2. John M. Christie
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  3. John T. M. Kennis
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  4. Gareth I. Jenkins
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  5. Tilo Mathes
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Corresponding author

Correspondence to Tilo Mathes.

Additional information

Electronic supplementary information (ESI) available: Additional FTIR spectroscopic data on H/D exchange and illumination dependent emission spectra are provided. See DOI: 10.1039/c4pp00246f

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Heilmann, M., Christie, J.M., Kennis, J.T.M. et al. Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy. Photochem Photobiol Sci 14, 252–257 (2015). https://doi.org/10.1039/c4pp00246f

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  • DOI: https://doi.org/10.1039/c4pp00246f

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