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  Aureochrome 1 illuminated: structural changes of a transcription factor probed by molecular spectroscopy

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): e103307, pp. 1-8. doi:10.1371/journal.pone.0103307.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-97D9-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-D0AF-E
Genre: Journal Article

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 Creators:
Kerruth, Silke, Author
Ataka, Kenichi, Author
Frey, Daniel1, Author              
Schlichting, Ilme1, Author              
Heberle, Joachim, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 2014-05-152014-06-292014-05-15
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: PLoS One
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 9 (7) Sequence Number: e103307 Start / End Page: 1 - 8 Identifier: ISSN: 1932-6203
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000277850