Evidence map›Paper›PMID 11964249›Full record

ArticleBiophysical journal2002

First evidence for phototropin-related blue-light receptors in prokaryotes.

Aba Losi, Eugenia Polverini, Benjamin Quest, Wolfgang Gärtner

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
16.6field-weighted citation impact, top 1% of its field
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

87 citing papers in PubMed, 271 citations in OpenAlex.

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  10. Responding to light signals: a comprehensive update on photomorphogenesis in cyanobacteria.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  11. Article
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  13. Residue alterations within a conserved hydrophobic pocket influence light, oxygen, voltage photoreceptor dark recovery.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
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  16. Comparing ultrafast excited state quenching of flavin 1,NPhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
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27 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 2 countries.

Aba LosiIstituto Nazionale per la Fisica della Materia and Department of Physics University of Parma, Parco Area delle Scienze 7/A, 43100 Parma, Italy. aba@mpi-muelheim.mpg.de
Eugenia Polverini
Benjamin Quest
Wolfgang Gärtner
Max Planck Society · DEMax Planck Institute of Biochemistry · DEUniversity of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A prokaryotic protein, YtvA from Bacillus subtilis, was found to possess a light, oxygen, voltage (LOV) domain sharing high homology with the photoactive, flavin mononucleotide (FMN)-binding LOV domains of phototropins (phot), blue-light photoreceptors for phototropism in higher plants. Computer-based three-dimensional modeling suggests that YtvA-LOV binds FMN in a similar pocket as phot-LOVs. Recombinant YtvA indeed exhibits the same spectroscopical features and blue-light-induced photochemistry as phot-LOVs, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct (Thio383). By means of laser-flash photolysis and time-resolved optoacoustic experiments, we measured the quantum yield of formation for Thio383, Phi(Thio) = 0.49, and the enthalpy change, DeltaH(Thio) = 135 kJ/mol, with respect to the parent state. The formation of Thio383 is accompanied by a considerable volume contraction, DeltaV(Thio) = -13.5 ml/mol. Similar to phot-LOVs, Thio383 is formed from the decay of a red-shifted transient species, T650, within 2 micros. In both YtvA and free FMN, this transient has an enthalpy content of approximately 200 kJ/mol, and its formation is accompanied by a small contraction, DeltaV(T) approximately -1.5 ml/mol, supporting the assignment of T650 to the FMN triplet state, as suggested by spectroscopical evidences. These are the first studies indicating that phototropin-related, blue-light receptors may exist also in prokaryotes, besides constituting a steadily growing family in plants.

Indexed as

Drosophila ProteinsEye ProteinsPhotoreceptor Cells, InvertebrateAmino Acid SequenceArabidopsisArabidopsis ProteinsBacillus subtilisBacterial ProteinsBiological ClocksCryptochromesFlavoproteinsLightModels, MolecularMolecular Sequence DataPhotochemistryPhotolysisArabidopsis ProteinsBacterial ProteinsCRY1 protein, Arabidopsiscry protein, DrosophilaCryptochromesDrosophila ProteinsEye ProteinsFlavoproteinsReceptors, G-Protein-Coupled

Identifiers

PMID11964249
PMCPMC1302051
OpenAlexW2088145350

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.