Journal Article

FZJ-2022-00320

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species

Smolentseva, A. ; Goncharov, I. M. ; Yudenko, A. ; Bogorodskiy, A. ; Semenov, O. ; Nazarenko, V. V. ; Borshchevskiy, V.FZJ* ; Fonin, A. V. ; Remeeva, A. ; Jaeger, K.-E.FZJ* ; Krauss, U.FZJ* ; Gordeliy, V.FZJ* ; Gushchin, I. (Corresponding author)

2021
Royal Society of Chemistry Cambridge

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Please use a persistent id in citations: http://hdl.handle.net/2128/30151  doi:10.1007/s43630-021-00138-3

Abstract: Light-oxygen-voltage (LOV) domains are common photosensory modules that found many applications in fluorescence microscopy and optogenetics. Here, we show that the Chloroflexus aggregans LOV domain can bind different flavin species (lumichrome, LC; riboflavin, RF; flavin mononucleotide, FMN; flavin adenine dinucleotide, FAD) during heterologous expression and that its physicochemical properties depend strongly on the nature of the bound flavin. We show that whereas the dissociation constants for different chromophores are similar, the melting temperature of the protein reconstituted with single flavin species varies from ~ 60 °C for LC to ~ 81 °C for FMN, and photobleaching half-times vary almost 100-fold. These observations serve as a caution for future studies of LOV domains in non-native conditions yet raise the possibility of fine-tuning various properties of LOV-based fluorescent probes and optogenetic tools by manipulating the chromophore composition.

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Contributing Institute(s):

1. Institut für Molekulare Enzymtechnologie (HHUD) (IMET)
2. Biotechnologie (IBG-1)
3. Strukturbiochemie (IBI-7)

Research Program(s):

1. 2171 - Biological and environmental resources for sustainable use (POF4-217) (POF4-217)
2. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2021

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