Kerruth, S; Ataka, K; Frey, D; Schlichting, I; Heberle, J
(2014)
Aureochrome 1 illuminated: structural changes of a transcription factor probed by molecular spectroscopy.
PLoS One, 9 (7).
ISSN 1932-6203
https://doi.org/10.1371/journal.pone.0103307
SGUL Authors: Kerruth, Silke
Abstract
Aureochrome 1 from Vaucheria frigida is a recently identified blue-light receptor that acts as a transcription factor. The protein comprises a photosensitive light-, oxygen- and voltage-sensitive (LOV) domain and a basic zipper (bZIP) domain that binds DNA rendering aureochrome 1 a prospective optogenetic tool. Here, we studied the photoreaction of full-length aureochrome 1 by molecular spectroscopy. The kinetics of the decay of the red-shifted triplet state and the blue-shifted signaling state were determined by time-resolved UV/Vis spectroscopy. It is shown that the presence of the bZIP domain further prolongs the lifetime of the LOV390 signaling state in comparison to the isolated LOV domain whereas bound DNA does not influence the photocycle kinetics. The light-dark Fourier transform infrared (FTIR) difference spectrum shows the characteristic features of the flavin mononucleotide chromophore except that the S-H stretching vibration of cysteine 254, which is involved in the formation of the thio-adduct state, is significantly shifted to lower frequencies compared to other LOV domains. The presence of the target DNA influences the light-induced FTIR difference spectrum of aureochrome 1. Vibrational bands that can be assigned to arginine and lysine side chains as well to the phosphate backbone, indicate crucial changes in interactions between transcription factor and DNA.
Item Type: |
Article
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Additional Information: |
© 2014 Kerruth et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
Keywords: |
Algal Proteins, Binding Sites, Cryptochromes, DNA, Kinetics, Models, Molecular, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, Structural Homology, Protein, Transcription Factors, Algal Proteins, Transcription Factors, DNA, Spectroscopy, Fourier Transform Infrared, Binding Sites, Protein Structure, Secondary, Structural Homology, Protein, Kinetics, Models, Molecular, Cryptochromes, General Science & Technology, MD Multidisciplinary |
SGUL Research Institute / Research Centre: |
Academic Structure > Molecular and Clinical Sciences Research Institute (MCS) |
Journal or Publication Title: |
PLoS One |
Article Number: |
e103307 |
ISSN: |
1932-6203 |
Language: |
eng |
Dates: |
Date | Event |
---|
24 July 2014 | Published | 29 June 2014 | Accepted |
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Publisher License: |
Creative Commons: Attribution 4.0 |
PubMed ID: |
25058114 |
![](http://static.pubmed.gov/portal/portal3rc.fcgi/2745237/img/27842) |
Go to PubMed abstract |
URI: |
https://openaccess.sgul.ac.uk/id/eprint/109126 |
Publisher's version: |
https://doi.org/10.1371/journal.pone.0103307 |
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