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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| Veröffentlicht in: | Photochemical & photobiological sciences 2021-12, Vol.20 (12), p.1645-1656 |
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| creator | 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 |
| description | 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 |
| doi_str_mv | 10.1007/s43630-021-00138-3 |
| format | Article |
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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</description><identifier>ISSN: 1474-905X</identifier><identifier>EISSN: 1474-9092</identifier><identifier>DOI: 10.1007/s43630-021-00138-3</identifier><identifier>PMID: 34796467</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Biochemistry ; Biochemistry & Molecular Biology ; Biomaterials ; Biophysics ; Chemistry ; Chemistry and Materials Science ; Chemistry, Physical ; Chloroflexus ; Flavin Mononucleotide ; Flavin-Adenine Dinucleotide ; Life Sciences & Biomedicine ; Original Papers ; Oxygen ; Physical Chemistry ; Physical Sciences ; Plant Sciences ; Riboflavin ; Science & Technology</subject><ispartof>Photochemical & photobiological sciences, 2021-12, Vol.20 (12), p.1645-1656</ispartof><rights>The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology 2021</rights><rights>2021. The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>2</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000720258200001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c391t-d23bc7c70897542d3b8004c6cabbbeeb313bd6882786a84dc6abede3bdb838243</citedby><cites>FETCH-LOGICAL-c391t-d23bc7c70897542d3b8004c6cabbbeeb313bd6882786a84dc6abede3bdb838243</cites><orcidid>0000-0002-5348-6070 ; 0000-0003-4398-9712 ; 0000-0003-4469-2531 ; 0000-0003-3977-3679 ; 0000-0001-9470-0013 ; 0000-0001-8966-9146 ; 0000-0002-7589-7823</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s43630-021-00138-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s43630-021-00138-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,782,786,27933,27934,39267,41497,42566,51328</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34796467$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Smolentseva, Anastasia</creatorcontrib><creatorcontrib>Goncharov, Ivan M.</creatorcontrib><creatorcontrib>Yudenko, Anna</creatorcontrib><creatorcontrib>Bogorodskiy, Andrey</creatorcontrib><creatorcontrib>Semenov, Oleg</creatorcontrib><creatorcontrib>Nazarenko, Vera V.</creatorcontrib><creatorcontrib>Borshchevskiy, Valentin</creatorcontrib><creatorcontrib>Fonin, Alexander V.</creatorcontrib><creatorcontrib>Remeeva, Alina</creatorcontrib><creatorcontrib>Jaeger, Karl-Erich</creatorcontrib><creatorcontrib>Krauss, Ulrich</creatorcontrib><creatorcontrib>Gordeliy, Valentin</creatorcontrib><creatorcontrib>Gushchin, Ivan</creatorcontrib><title>Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species</title><title>Photochemical & photobiological sciences</title><addtitle>Photochem Photobiol Sci</addtitle><addtitle>PHOTOCH PHOTOBIO SCI</addtitle><addtitle>Photochem Photobiol Sci</addtitle><description>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</description><subject>Biochemistry</subject><subject>Biochemistry & Molecular Biology</subject><subject>Biomaterials</subject><subject>Biophysics</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry, Physical</subject><subject>Chloroflexus</subject><subject>Flavin Mononucleotide</subject><subject>Flavin-Adenine Dinucleotide</subject><subject>Life Sciences & Biomedicine</subject><subject>Original Papers</subject><subject>Oxygen</subject><subject>Physical Chemistry</subject><subject>Physical Sciences</subject><subject>Plant Sciences</subject><subject>Riboflavin</subject><subject>Science & Technology</subject><issn>1474-905X</issn><issn>1474-9092</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><sourceid>EIF</sourceid><recordid>eNqNkMtu1TAURS1ERR_wAwyQh0go1K8kzhBFpUW6UieAmFl-nNybKrGD7UD797hNuUPEyFs-ax_ZC6G3lHykhLSXSfCGk4owWhFCuaz4C3RGRSuqjnTs5THXP07ReUp3BapF075Cp1y0XVPiGfJX9znCDNjBAt6Bt4DDgPvDFGIYJrhfE9b7fYS99gnvbr9jF2Y9epwPEOdQYe0dXg4hh5S1GacxP-DwNMUmrGU2TPpXwdMCdoT0Gp0Mekrw5vm8QN8-X33tb6rd7fWX_tOusryjuXKMG9valsiurQVz3EhChG2sNsYAGE65cY2UrJWNlsLZRhtwUC6N5JIJfoHeb3uXGH6ukLKax2RhmrSHsCbF6q6jkjadLCjbUBtDShEGtcRx1vFBUaIePavNsyqe1ZNnxUvp3fP-1czgjpW_YgsgN-A3mDCk8vdi9oiRspYRVktWEqH9mHUeg--LsVyqH_6_Wmi-0akQfg9R3YU1-iL3X-__A46rqzI</recordid><startdate>20211201</startdate><enddate>20211201</enddate><creator>Smolentseva, Anastasia</creator><creator>Goncharov, Ivan M.</creator><creator>Yudenko, Anna</creator><creator>Bogorodskiy, Andrey</creator><creator>Semenov, Oleg</creator><creator>Nazarenko, Vera V.</creator><creator>Borshchevskiy, Valentin</creator><creator>Fonin, Alexander V.</creator><creator>Remeeva, Alina</creator><creator>Jaeger, Karl-Erich</creator><creator>Krauss, Ulrich</creator><creator>Gordeliy, Valentin</creator><creator>Gushchin, Ivan</creator><general>Springer International Publishing</general><general>Springer Nature</general><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-5348-6070</orcidid><orcidid>https://orcid.org/0000-0003-4398-9712</orcidid><orcidid>https://orcid.org/0000-0003-4469-2531</orcidid><orcidid>https://orcid.org/0000-0003-3977-3679</orcidid><orcidid>https://orcid.org/0000-0001-9470-0013</orcidid><orcidid>https://orcid.org/0000-0001-8966-9146</orcidid><orcidid>https://orcid.org/0000-0002-7589-7823</orcidid></search><sort><creationdate>20211201</creationdate><title>Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species</title><author>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</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-d23bc7c70897542d3b8004c6cabbbeeb313bd6882786a84dc6abede3bdb838243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Biochemistry</topic><topic>Biochemistry & Molecular Biology</topic><topic>Biomaterials</topic><topic>Biophysics</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry, Physical</topic><topic>Chloroflexus</topic><topic>Flavin Mononucleotide</topic><topic>Flavin-Adenine Dinucleotide</topic><topic>Life Sciences & Biomedicine</topic><topic>Original Papers</topic><topic>Oxygen</topic><topic>Physical Chemistry</topic><topic>Physical Sciences</topic><topic>Plant Sciences</topic><topic>Riboflavin</topic><topic>Science & Technology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smolentseva, Anastasia</creatorcontrib><creatorcontrib>Goncharov, Ivan M.</creatorcontrib><creatorcontrib>Yudenko, Anna</creatorcontrib><creatorcontrib>Bogorodskiy, Andrey</creatorcontrib><creatorcontrib>Semenov, Oleg</creatorcontrib><creatorcontrib>Nazarenko, Vera V.</creatorcontrib><creatorcontrib>Borshchevskiy, Valentin</creatorcontrib><creatorcontrib>Fonin, Alexander V.</creatorcontrib><creatorcontrib>Remeeva, Alina</creatorcontrib><creatorcontrib>Jaeger, Karl-Erich</creatorcontrib><creatorcontrib>Krauss, Ulrich</creatorcontrib><creatorcontrib>Gordeliy, Valentin</creatorcontrib><creatorcontrib>Gushchin, Ivan</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 2021</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Photochemical & photobiological sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smolentseva, Anastasia</au><au>Goncharov, Ivan M.</au><au>Yudenko, Anna</au><au>Bogorodskiy, Andrey</au><au>Semenov, Oleg</au><au>Nazarenko, Vera V.</au><au>Borshchevskiy, Valentin</au><au>Fonin, Alexander V.</au><au>Remeeva, Alina</au><au>Jaeger, Karl-Erich</au><au>Krauss, Ulrich</au><au>Gordeliy, Valentin</au><au>Gushchin, Ivan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species</atitle><jtitle>Photochemical & photobiological sciences</jtitle><stitle>Photochem Photobiol Sci</stitle><stitle>PHOTOCH PHOTOBIO SCI</stitle><addtitle>Photochem Photobiol Sci</addtitle><date>2021-12-01</date><risdate>2021</risdate><volume>20</volume><issue>12</issue><spage>1645</spage><epage>1656</epage><pages>1645-1656</pages><issn>1474-905X</issn><eissn>1474-9092</eissn><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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| subjects | Biochemistry Biochemistry & Molecular Biology Biomaterials Biophysics Chemistry Chemistry and Materials Science Chemistry, Physical Chloroflexus Flavin Mononucleotide Flavin-Adenine Dinucleotide Life Sciences & Biomedicine Original Papers Oxygen Physical Chemistry Physical Sciences Plant Sciences Riboflavin Science & Technology |
| title | Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species |
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