This title appears in the Scientific Report :
2021
Please use the identifier:
http://dx.doi.org/10.1007/s43630-021-00138-3 in citations.
Please use the identifier: http://hdl.handle.net/2128/30151 in citations.
Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species
Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species
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...
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Personal Name(s): | Smolentseva, Anastasia |
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Goncharov, Ivan M. / Yudenko, Anna / Bogorodskiy, Andrey / Semenov, Oleg / Nazarenko, Vera V. / Borshchevskiy, Valentin / Fonin, Alexander V. / Remeeva, Alina / Jaeger, Karl-Erich / Krauss, Ulrich / Gordeliy, Valentin / Gushchin, Ivan (Corresponding author) | |
Contributing Institute: |
Biotechnologie; IBG-1 Institut für Molekulare Enzymtechnologie (HHUD); IMET |
Published in: | Photochemical & photobiological sciences, 20 (2021) 12, S. 1645 - 1656 |
Imprint: |
Cambridge
Royal Society of Chemistry
2021
|
DOI: |
10.1007/s43630-021-00138-3 |
Document Type: |
Journal Article |
Research Program: |
Biological and environmental resources for sustainable use |
Link: |
Get full text Published on 2021-12-18. Available in OpenAccess from 2022-12-18. |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/30151 in citations.
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. |