Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species
| Autor: | Anastasia Smolentseva, Andrey Bogorodskiy, Ivan M. Goncharov, Valentin Borshchevskiy, Alexander V. Fonin, Karl-Erich Jaeger, Alina Remeeva, Valentin Gordeliy, Ivan Gushchin, Anna Yudenko, Vera V. Nazarenko, Oleg Semenov, Ulrich Krauss |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Flavin adenine dinucleotide
Flavin Mononucleotide Riboflavin Flavin mononucleotide Flavin group Chromophore medicine.disease_cause Photobleaching Fluorescence Chloroflexus Oxygen chemistry.chemical_compound chemistry Flavin-Adenine Dinucleotide medicine Biophysics heterocyclic compounds Physical and Theoretical Chemistry ddc:620 Chloroflexus aggregans |
| Zdroj: | Photochemical & photobiological sciences 20(12), 1645-1656 (2021). doi:10.1007/s43630-021-00138-3 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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