Journal Article

PreJuSER-38378

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Functional variations among LOV domains as revealed by FTIR difference spectroscopy

Bednarz, T.FZJ* ; Losi, A. ; Gärtner, W. ; Hegemann, P. ; Heberle, J.FZJ*

2004
Royal Society of Chemistry Cambridge

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Please use a persistent id in citations: doi:10.1039/b400976b

Abstract: The two LOV domains, LOV1 and LOV2, from Chlamydomonas reinhardtii were investigated by light-induced FT-IR difference spectroscopy and compared to the LOV domain of Bacillus subtilis (YtvA-LOV). It is shown that the two S-H conformations of the reactive LOV1 cysteine C57(1) are exposed to environments of different hydrogen bonding strength. Thus, the two rotamer configurations of C57 might be related to the fact that the triplet state decays bi-exponentially into the LOV1-390 photoproduct. Exchange of the two other cysteines of LOV1 (C32S and C83S) does not alter the S-H stretching band providing evidence that this band feature arises solely from C57. The reactive cysteine of LOV2 from Chlamydomonas reinhardtii (C250) and of YtvA-LOV (C62) exhibit both a homogenous S-H stretching vibrational band which suggests a single conformer of the amino acid side chain. Finally, the FT-IR difference spectrum of YtvA from Bacillus subtilis comprising the light absorbing LOV domain and the putative signaling STAS (sulfate transporter/antisigma-factor antagonist) domain, reveals conformational changes in the latter after blue-light excitation.

Keyword(s): Animals (MeSH) ; Bacillus subtilis: physiology (MeSH) ; Bacillus subtilis: radiation effects (MeSH) ; Bacterial Proteins: chemistry (MeSH) ; Bacterial Proteins: genetics (MeSH) ; Bacterial Proteins: physiology (MeSH) ; Chlamydomonas reinhardtii: physiology (MeSH) ; Chlamydomonas reinhardtii: radiation effects (MeSH) ; Crystallography, X-Ray (MeSH) ; Protein Conformation (MeSH) ; Spectrometry, Fluorescence (MeSH) ; Spectroscopy, Fourier Transform Infrared: methods (MeSH) ; Bacterial Proteins ; J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biologische Strukturforschung (IBI-2)

Research Program(s):

1. Neurowissenschaften (L01)

Appears in the scientific report 2004

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