Evidence map›Paper›PMID 34796467›Full record

ArticlePhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology2021

Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species.

Anastasia Smolentseva, Ivan M Goncharov, Anna Yudenko, Andrey Bogorodskiy, Oleg Semenov, Vera V Nazarenko, Valentin Borshchevskiy, Alexander V Fonin, Alina Remeeva, Karl-Erich Jaeger and 3 more

Abstract read
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In one paragraph

Article in Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Reengineering of a flavin-binding fluorescent protein using ProteinMPNN.Protein science : a publication of the Protein Society · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Anastasia SmolentsevaResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Ivan M GoncharovResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Anna YudenkoResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Andrey BogorodskiyResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Oleg SemenovResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Vera V NazarenkoResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Valentin BorshchevskiyResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Alexander V FoninInstitute of Cytology, Russian Academy of Sciences, 194064, Saint Petersburg, Russia.
Alina RemeevaResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Karl-Erich JaegerInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany.
Ulrich KraussInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany.
Valentin GordeliyResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Ivan GushchinResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia. ivan.gushchin@phystech.edu.ORCID http://orcid.org/0000-0002-5348-6070

Funding

Russian Science Foundation 21-64-00018
6 · The paper itself

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.

Indexed as

ChloroflexusOxygenFlavin-Adenine DinucleotideFlavin MononucleotideRiboflavinFlavin-Adenine DinucleotideFlavin MononucleotideOxygenRiboflavinChromophoreFlavin-based fluorescent proteinFlavin mononucleotideLOV domainProtein–ligand interactionsRiboflavinThermal stability

Identifiers

PMID34796467

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.