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...
Ausführliche Beschreibung
Autor*in: |
Smolentseva, Anastasia [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2021 |
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Schlagwörter: |
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Anmerkung: |
© The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 |
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Übergeordnetes Werk: |
Enthalten in: Photochemical & photobiological sciences - Heidelberg : Springer, 2002, 20(2021), 12 vom: 18. Nov., Seite 1645-1656 |
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Übergeordnetes Werk: |
volume:20 ; year:2021 ; number:12 ; day:18 ; month:11 ; pages:1645-1656 |
Links: |
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DOI / URN: |
10.1007/s43630-021-00138-3 |
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Katalog-ID: |
SPR045780188 |
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100 | 1 | |a Smolentseva, Anastasia |e verfasserin |4 aut | |
245 | 1 | 0 | |a Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species |
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520 | |a 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. Graphical abstract | ||
650 | 4 | |a LOV domain |7 (dpeaa)DE-He213 | |
650 | 4 | |a Flavin-based fluorescent protein |7 (dpeaa)DE-He213 | |
650 | 4 | |a Riboflavin |7 (dpeaa)DE-He213 | |
650 | 4 | |a Flavin mononucleotide |7 (dpeaa)DE-He213 | |
650 | 4 | |a Chromophore |7 (dpeaa)DE-He213 | |
650 | 4 | |a Thermal stability |7 (dpeaa)DE-He213 | |
650 | 4 | |a Protein–ligand interactions |7 (dpeaa)DE-He213 | |
700 | 1 | |a Goncharov, Ivan M. |4 aut | |
700 | 1 | |a Yudenko, Anna |4 aut | |
700 | 1 | |a Bogorodskiy, Andrey |4 aut | |
700 | 1 | |a Semenov, Oleg |4 aut | |
700 | 1 | |a Nazarenko, Vera V. |4 aut | |
700 | 1 | |a Borshchevskiy, Valentin |4 aut | |
700 | 1 | |a Fonin, Alexander V. |4 aut | |
700 | 1 | |a Remeeva, Alina |4 aut | |
700 | 1 | |a Jaeger, Karl-Erich |4 aut | |
700 | 1 | |a Krauss, Ulrich |4 aut | |
700 | 1 | |a Gordeliy, Valentin |4 aut | |
700 | 1 | |a Gushchin, Ivan |0 (orcid)0000-0002-5348-6070 |4 aut | |
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912 | |a GBV_ILN_161 | ||
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912 | |a GBV_ILN_281 | ||
912 | |a GBV_ILN_285 | ||
912 | |a GBV_ILN_293 | ||
912 | |a GBV_ILN_370 | ||
912 | |a GBV_ILN_374 | ||
912 | |a GBV_ILN_602 | ||
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912 | |a GBV_ILN_2009 | ||
912 | |a GBV_ILN_2010 | ||
912 | |a GBV_ILN_2011 | ||
912 | |a GBV_ILN_2014 | ||
912 | |a GBV_ILN_2015 | ||
912 | |a GBV_ILN_2020 | ||
912 | |a GBV_ILN_2021 | ||
912 | |a GBV_ILN_2025 | ||
912 | |a GBV_ILN_2026 | ||
912 | |a GBV_ILN_2027 | ||
912 | |a GBV_ILN_2031 | ||
912 | |a GBV_ILN_2034 | ||
912 | |a GBV_ILN_2037 | ||
912 | |a GBV_ILN_2038 | ||
912 | |a GBV_ILN_2039 | ||
912 | |a GBV_ILN_2044 | ||
912 | |a GBV_ILN_2048 | ||
912 | |a GBV_ILN_2049 | ||
912 | |a GBV_ILN_2050 | ||
912 | |a GBV_ILN_2055 | ||
912 | |a GBV_ILN_2056 | ||
912 | |a GBV_ILN_2057 | ||
912 | |a GBV_ILN_2059 | ||
912 | |a GBV_ILN_2061 | ||
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912 | |a GBV_ILN_2068 | ||
912 | |a GBV_ILN_2088 | ||
912 | |a GBV_ILN_2093 | ||
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912 | |a GBV_ILN_2111 | ||
912 | |a GBV_ILN_2112 | ||
912 | |a GBV_ILN_2113 | ||
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912 | |a GBV_ILN_2122 | ||
912 | |a GBV_ILN_2129 | ||
912 | |a GBV_ILN_2143 | ||
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912 | |a GBV_ILN_2147 | ||
912 | |a GBV_ILN_2148 | ||
912 | |a GBV_ILN_2152 | ||
912 | |a GBV_ILN_2153 | ||
912 | |a GBV_ILN_2190 | ||
912 | |a GBV_ILN_2232 | ||
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912 | |a GBV_ILN_2470 | ||
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912 | |a GBV_ILN_4324 | ||
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10.1007/s43630-021-00138-3 doi (DE-627)SPR045780188 (SPR)s43630-021-00138-3-e DE-627 ger DE-627 rakwb eng Smolentseva, Anastasia verfasserin aut Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 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. Graphical abstract LOV domain (dpeaa)DE-He213 Flavin-based fluorescent protein (dpeaa)DE-He213 Riboflavin (dpeaa)DE-He213 Flavin mononucleotide (dpeaa)DE-He213 Chromophore (dpeaa)DE-He213 Thermal stability (dpeaa)DE-He213 Protein–ligand interactions (dpeaa)DE-He213 Goncharov, Ivan M. aut Yudenko, Anna aut Bogorodskiy, Andrey aut Semenov, Oleg aut Nazarenko, Vera V. aut Borshchevskiy, Valentin aut Fonin, Alexander V. aut Remeeva, Alina aut Jaeger, Karl-Erich aut Krauss, Ulrich aut Gordeliy, Valentin aut Gushchin, Ivan (orcid)0000-0002-5348-6070 aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 20(2021), 12 vom: 18. Nov., Seite 1645-1656 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:20 year:2021 number:12 day:18 month:11 pages:1645-1656 https://dx.doi.org/10.1007/s43630-021-00138-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 20 2021 12 18 11 1645-1656 |
spelling |
10.1007/s43630-021-00138-3 doi (DE-627)SPR045780188 (SPR)s43630-021-00138-3-e DE-627 ger DE-627 rakwb eng Smolentseva, Anastasia verfasserin aut Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 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. Graphical abstract LOV domain (dpeaa)DE-He213 Flavin-based fluorescent protein (dpeaa)DE-He213 Riboflavin (dpeaa)DE-He213 Flavin mononucleotide (dpeaa)DE-He213 Chromophore (dpeaa)DE-He213 Thermal stability (dpeaa)DE-He213 Protein–ligand interactions (dpeaa)DE-He213 Goncharov, Ivan M. aut Yudenko, Anna aut Bogorodskiy, Andrey aut Semenov, Oleg aut Nazarenko, Vera V. aut Borshchevskiy, Valentin aut Fonin, Alexander V. aut Remeeva, Alina aut Jaeger, Karl-Erich aut Krauss, Ulrich aut Gordeliy, Valentin aut Gushchin, Ivan (orcid)0000-0002-5348-6070 aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 20(2021), 12 vom: 18. Nov., Seite 1645-1656 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:20 year:2021 number:12 day:18 month:11 pages:1645-1656 https://dx.doi.org/10.1007/s43630-021-00138-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 20 2021 12 18 11 1645-1656 |
allfields_unstemmed |
10.1007/s43630-021-00138-3 doi (DE-627)SPR045780188 (SPR)s43630-021-00138-3-e DE-627 ger DE-627 rakwb eng Smolentseva, Anastasia verfasserin aut Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 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. Graphical abstract LOV domain (dpeaa)DE-He213 Flavin-based fluorescent protein (dpeaa)DE-He213 Riboflavin (dpeaa)DE-He213 Flavin mononucleotide (dpeaa)DE-He213 Chromophore (dpeaa)DE-He213 Thermal stability (dpeaa)DE-He213 Protein–ligand interactions (dpeaa)DE-He213 Goncharov, Ivan M. aut Yudenko, Anna aut Bogorodskiy, Andrey aut Semenov, Oleg aut Nazarenko, Vera V. aut Borshchevskiy, Valentin aut Fonin, Alexander V. aut Remeeva, Alina aut Jaeger, Karl-Erich aut Krauss, Ulrich aut Gordeliy, Valentin aut Gushchin, Ivan (orcid)0000-0002-5348-6070 aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 20(2021), 12 vom: 18. Nov., Seite 1645-1656 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:20 year:2021 number:12 day:18 month:11 pages:1645-1656 https://dx.doi.org/10.1007/s43630-021-00138-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 20 2021 12 18 11 1645-1656 |
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10.1007/s43630-021-00138-3 doi (DE-627)SPR045780188 (SPR)s43630-021-00138-3-e DE-627 ger DE-627 rakwb eng Smolentseva, Anastasia verfasserin aut Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 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. Graphical abstract LOV domain (dpeaa)DE-He213 Flavin-based fluorescent protein (dpeaa)DE-He213 Riboflavin (dpeaa)DE-He213 Flavin mononucleotide (dpeaa)DE-He213 Chromophore (dpeaa)DE-He213 Thermal stability (dpeaa)DE-He213 Protein–ligand interactions (dpeaa)DE-He213 Goncharov, Ivan M. aut Yudenko, Anna aut Bogorodskiy, Andrey aut Semenov, Oleg aut Nazarenko, Vera V. aut Borshchevskiy, Valentin aut Fonin, Alexander V. aut Remeeva, Alina aut Jaeger, Karl-Erich aut Krauss, Ulrich aut Gordeliy, Valentin aut Gushchin, Ivan (orcid)0000-0002-5348-6070 aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 20(2021), 12 vom: 18. Nov., Seite 1645-1656 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:20 year:2021 number:12 day:18 month:11 pages:1645-1656 https://dx.doi.org/10.1007/s43630-021-00138-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 20 2021 12 18 11 1645-1656 |
allfieldsSound |
10.1007/s43630-021-00138-3 doi (DE-627)SPR045780188 (SPR)s43630-021-00138-3-e DE-627 ger DE-627 rakwb eng Smolentseva, Anastasia verfasserin aut Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 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. Graphical abstract LOV domain (dpeaa)DE-He213 Flavin-based fluorescent protein (dpeaa)DE-He213 Riboflavin (dpeaa)DE-He213 Flavin mononucleotide (dpeaa)DE-He213 Chromophore (dpeaa)DE-He213 Thermal stability (dpeaa)DE-He213 Protein–ligand interactions (dpeaa)DE-He213 Goncharov, Ivan M. aut Yudenko, Anna aut Bogorodskiy, Andrey aut Semenov, Oleg aut Nazarenko, Vera V. aut Borshchevskiy, Valentin aut Fonin, Alexander V. aut Remeeva, Alina aut Jaeger, Karl-Erich aut Krauss, Ulrich aut Gordeliy, Valentin aut Gushchin, Ivan (orcid)0000-0002-5348-6070 aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 20(2021), 12 vom: 18. Nov., Seite 1645-1656 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:20 year:2021 number:12 day:18 month:11 pages:1645-1656 https://dx.doi.org/10.1007/s43630-021-00138-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 20 2021 12 18 11 1645-1656 |
language |
English |
source |
Enthalten in Photochemical & photobiological sciences 20(2021), 12 vom: 18. Nov., Seite 1645-1656 volume:20 year:2021 number:12 day:18 month:11 pages:1645-1656 |
sourceStr |
Enthalten in Photochemical & photobiological sciences 20(2021), 12 vom: 18. Nov., Seite 1645-1656 volume:20 year:2021 number:12 day:18 month:11 pages:1645-1656 |
format_phy_str_mv |
Article |
institution |
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topic_facet |
LOV domain Flavin-based fluorescent protein Riboflavin Flavin mononucleotide Chromophore Thermal stability Protein–ligand interactions |
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container_title |
Photochemical & photobiological sciences |
authorswithroles_txt_mv |
Smolentseva, Anastasia @@aut@@ Goncharov, Ivan M. @@aut@@ Yudenko, Anna @@aut@@ Bogorodskiy, Andrey @@aut@@ Semenov, Oleg @@aut@@ Nazarenko, Vera V. @@aut@@ Borshchevskiy, Valentin @@aut@@ Fonin, Alexander V. @@aut@@ Remeeva, Alina @@aut@@ Jaeger, Karl-Erich @@aut@@ Krauss, Ulrich @@aut@@ Gordeliy, Valentin @@aut@@ Gushchin, Ivan @@aut@@ |
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2021-11-18T00:00:00Z |
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author |
Smolentseva, Anastasia |
spellingShingle |
Smolentseva, Anastasia misc LOV domain misc Flavin-based fluorescent protein misc Riboflavin misc Flavin mononucleotide misc Chromophore misc Thermal stability misc Protein–ligand interactions Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species |
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Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species LOV domain (dpeaa)DE-He213 Flavin-based fluorescent protein (dpeaa)DE-He213 Riboflavin (dpeaa)DE-He213 Flavin mononucleotide (dpeaa)DE-He213 Chromophore (dpeaa)DE-He213 Thermal stability (dpeaa)DE-He213 Protein–ligand interactions (dpeaa)DE-He213 |
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misc LOV domain misc Flavin-based fluorescent protein misc Riboflavin misc Flavin mononucleotide misc Chromophore misc Thermal stability misc Protein–ligand interactions |
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misc LOV domain misc Flavin-based fluorescent protein misc Riboflavin misc Flavin mononucleotide misc Chromophore misc Thermal stability misc Protein–ligand interactions |
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Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species |
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Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species |
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Smolentseva, Anastasia |
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Smolentseva, Anastasia 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 |
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title_sort |
extreme dependence of chloroflexus aggregans lov domain thermo- and photostability on the bound flavin species |
title_auth |
Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species |
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. Graphical abstract © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 |
abstractGer |
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. Graphical abstract © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 |
abstract_unstemmed |
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. Graphical abstract © The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021 |
collection_details |
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container_issue |
12 |
title_short |
Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species |
url |
https://dx.doi.org/10.1007/s43630-021-00138-3 |
remote_bool |
true |
author2 |
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 |
author2Str |
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 |
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hochschulschrift_bool |
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doi_str |
10.1007/s43630-021-00138-3 |
up_date |
2024-07-03T18:14:25.958Z |
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|
score |
7.4016542 |