ArticleBiophysical journal2009
Light signal transduction pathway from flavin chromophore to the J alpha helix of Arabidopsis phototropin1.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
- QM/MM Calculated Triplet-Singlet Infrared Difference Spectra of LOV2 Photoreceptor Domains and FMN in Solution.ACS omega · 2026Article
- β-sheets mediate the conformational change and allosteric signal transmission between the AsLOV2 termini.Journal of computational chemistry · 2024Article
- Light-inducible protein degradation ineLife · 2024Article
- How Aqueous Solvation Impacts the Frequencies and Intensities of Infrared Absorption Bands in Flavin: The Quest for a Suitable Solvent Model.Molecules (Basel, Switzerland) · 2024Article
- Dynamics of hydrogen bonds in the secondary structures of allosteric proteinComputational and structural biotechnology journal · 2022Article
- Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1.Scientific reports · 2021Article
- Unraveling the Mechanism of a LOV Domain Optogenetic Sensor: A Glutamine Lever Induces Unfolding of the Jα Helix.ACS chemical biology · 2020Article
- Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain ofACS omega · 2019Article
- Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes.Nucleic acids research · 2016Article
- Intramolecular co-action of two independent photosensory modules in the fern phytochrome 3.Plant signaling & behavior · 2015Article
- The amino-terminal helix modulates light-activated conformational changes in AsLOV2.Journal of molecular biology · 2012Article
- Mutations in N-terminal flanking region of blue light-sensing light-oxygen and voltage 2 (LOV2) domain disrupt its repressive activity on kinase domain in the Chlamydomonas phototropin.The Journal of biological chemistry · 2012Article
- Function, structure and mechanism of bacterial photosensory LOV proteins.Nature reviews. Microbiology · 2011Review
- Light-induced structural changes of the LOV2 domains in various phototropins revealed by FTIR spectroscopy.Biophysics (Nagoya-shi, Japan) · 2011Review
- Mechanism of signal transduction of the LOV2-Jα photosensor from Avena sativa.Nature communications · 2010Article
- Key dynamics of conserved asparagine in a cryptochrome/photolyase family protein by fourier transform infrared spectroscopy.Biochemistry · 2010Article
- Structural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria.The Journal of biological chemistry · 2010Article
- The primary photophysics of the Avena sativa phototropin 1 LOV2 domain observed with time-resolved emission spectroscopy.Photochemistry and photobiologyArticle
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6 authors.
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Abstract
In the plant blue-light sensor phototropin, illumination of the chromophoric LOV domains causes activation of the serine/threonine kinase domain. Flavin mononucleotide (FMN) is a chromophore molecule in the two LOV domains (LOV1 and LOV2), but only LOV2 is responsible for kinase activation. Previous studies reported an important role of an additional helix connected to the C-terminal of LOV2 (Jalpha helix) for the function of phototropin; however, it remains unclear how the Jalpha helix affects light-induced structural changes in LOV2. In this study we compared light-induced protein structural changes of the LOV2 domain of Arabidopsis phot1 in the absence (LOV2-core) and presence (LOV2-Jalpha) of the Jalpha helix by Fourier-transform infrared spectroscopy. Prominent peaks were observed only in the amide-I region (1650 (-)/1625 (+) cm(-1)) of LOV2-Jalpha at physiological temperatures (>/=260 K), corresponding to structural perturbation of the alpha-helix. The peaks were diminished by point mutation of functionally important amino acids such as Phe-556 between FMN and the beta-sheet, Gln-575 being hydrogen-bonded with FMN, and Ile-608 on the Jalpha helix. We thus conclude that a light signal is relayed from FMN through these amino acids and eventually changes the interaction between LOV2-core and the Jalpha helix in Arabidopsis phot1.
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