ArticleThe Journal of biological chemistry2012
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.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 52 citations in OpenAlex.
- Modulation of Phototropin Signalosome with Artificial Illumination Holds Great Potential in the Development of Climate-Smart Crops.Current genomics · 2021Review
- Lipid flippases as key players in plant adaptation to their environment.Nature plants · 2021Review
- In-cell infrared difference spectroscopy of LOV photoreceptors reveals structural responses to light altered in living cells.The Journal of biological chemistry · 2020Article
- Optogenetic control of protein binding using light-switchable nanobodies.Nature communications · 2020Article
- An optogenetic system to control membrane phospholipid asymmetry through flippase activation in budding yeast.Scientific reports · 2020Article
- Low-fluence blue light-induced phosphorylation of Zmphot1 mediates the first positive phototropism.Journal of experimental botany · 2019Article
- Engineering the phototropin photocycle improves photoreceptor performance and plant biomass production.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain ofACS omega · 2019Article
- Electron transfer pathways in a light, oxygen, voltage (LOV) protein devoid of the photoactive cysteine.Scientific reports · 2017Article
- Functional characterization of a constitutively active kinase variant ofThe Journal of biological chemistry · 2017Article
- Blue Light-excited Light-Oxygen-Voltage-sensing Domain 2 (LOV2) Triggers a Rearrangement of the Kinase Domain to Induce Phosphorylation Activity in Arabidopsis Phototropin1.The Journal of biological chemistry · 2016Article
- Blue-light-regulated transcription factor, Aureochrome, in photosynthetic stramenopiles.Journal of plant research · 2016Review
- Molecular mechanism of phototropin light signaling.Journal of plant research · 2016Review
- Signal transduction in light-oxygen-voltage receptors lacking the adduct-forming cysteine residue.Nature communications · 2015Article
- Plant flavoprotein photoreceptors.Plant & cell physiology · 2015Review
- Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations-implications for the understanding of LOV photoactivation.Frontiers in molecular biosciences · 2015Article
- Article
- Photo-sensitive degron variants for tuning protein stability by light.BMC systems biology · 2014Article
- Photochemistry of flavoprotein light sensors.Nature chemical biology · 2014Review
- Phototropin encoded by a single-copy gene mediates chloroplast photorelocation movements in the liverwort Marchantia polymorpha.Plant physiology · 2014Article
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8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phototropin is a light-regulated kinase that mediates a variety of photoresponses such as phototropism, chloroplast positioning, and stomata opening in plants to increase the photosynthetic efficiency. Blue light stimulus first induces local conformational changes in the chromophore-bearing light-oxygen and voltage 2 (LOV2) domain of phototropin, which in turn activates the serine/threonine (Ser/Thr) kinase domain in the C terminus. To examine the kinase activity of full-length phototropin conventionally, we employed the budding yeast Saccharomyces cerevisiae. In this organism, Ser/Thr kinases (Fpk1p and Fpk2p) that show high sequence similarity to the kinase domain of phototropins exist. First, we demonstrated that the phototropin from Chlamydomonas reinhardtii (CrPHOT) could complement loss of Fpk1p and Fpk2p to allow cell growth in yeast. Furthermore, this reaction was blue light-dependent, indicating that CrPHOT was indeed light-activated in yeast cells. We applied this system to a large scale screening for amino acid substitutions in CrPHOT that elevated the kinase activity in darkness. Consequently, we identified a cluster of mutations located in the N-terminal flanking region of LOV2 (R199C, L202L, D203N/G/V, L204P, T207I, and R210H). An in vitro phosphorylation assay confirmed that these mutations substantially reduced the repressive activity of LOV2 on the kinase domain in darkness. Furthermore, biochemical analyses of the representative T207I mutant demonstrated that the mutation affected neither spectral nor multimerization properties of CrPHOT. Hence, the N-terminal flanking region of LOV2, as is the case with the C-terminal flanking Jα region, appears to play a crucial role in the regulation of kinase activity in phototropin.
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