Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain

Salomon, Michael; Lempert, Ulrika; Rüdiger, Wolfhart

doi:10.1016/j.febslet.2004.06.081

Cited by 107 publications

(102 citation statements)

References 15 publications

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“…In contrast to the predominant light-sensing role of LOV2 (28), LOV1 shows minimal structural alterations upon photoexcitation (29,30) and is proposed to mediate receptor dimerization (31,32). In our structures, Ser-394 forms a hydrogen bond with Asn-401, directing the Ser hydroxyl away from the FMN ring.…”

Section: Discussionmentioning

confidence: 73%

Structural Tuning of the Fluorescent Protein iLOV for Improved Photostability

Christie

Hitomi

Arvai

et al. 2012

Journal of Biological Chemistry

137

199

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Background: iLOV is a fluorescent flavoprotein engineered from the plant blue light receptor phototropin. Results: Structures reveal altered protein-chromophore interactions within the flavin-binding cavity of iLOV when compared with its progenitors. Directed evolution further anchored the chromophore to increase iLOV photostability by an order of magnitude. Conclusion: Improving iLOV photostability by constraining its fluorophore establishes a framework for fine-tuning fluorescence. Significance: Enhanced photostability increases iLOV utility as an oxygen-independent fluorescent reporter.

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Section: Discussionmentioning

confidence: 73%

Structural Tuning of the Fluorescent Protein iLOV for Improved Photostability

Christie

Hitomi

Arvai

et al. 2012

Journal of Biological Chemistry

137

199

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“…Higher plant PHYs carry a typical double-PAS domain possibly involved in dimerization. Indeed, PHOT LOV domains dimerize in vitro (27,28). Thus it is quite possible that the LOV͞PAS domains of NEO in Mougeotia have evolved to play a role other than f lavin binding.…”

Section: Resultsmentioning

confidence: 99%

A chimeric photoreceptor gene, NEOCHROME, has arisen twice during plant evolution

Suetsugu

Mittmann

Wagner

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

153

149

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Although most plant species from algae to flowering plants use blue light for inducing phototropism and chloroplast movement, many ferns, some mosses, and green algae use red as well as blue light for the regulation of these responses, resulting in better sensitivity at low light levels. During their evolution, ferns have created a chimeric photoreceptor (phy3 in Adiantum) between phytochrome (phy) and phototropin (phot) enabling them to use red light effectively. We have identified two genes resembling Adiantum PHY3, NEOCHROME1 and NEOCHROME2 (MsNEO1 and MsNEO2), in the green alga Mougeotia scalaris, a plant famous for its light-regulated chloroplast movement. Like Adiantum PHY3, both MsNEO gene products show phytochrome-typical bilin binding and red͞far-red reversibility, the difference spectra matching the known action spectra of light-induced chloroplast movement in Mougeotia. Furthermore, both genes rescue red-light-induced chloroplast movement in Adiantum phy3 mutants, indicating functional equivalence. However, the fern and algal genes seem to have arisen independently in evolution, thus providing an intriguing example of convergent evolution. convergent evolution ͉ Mougeotia

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“…A similar mode of action has been reported for the LOV2 domain of Arabidopsis phot2. 12,14,15 The LOV1 domain, by contrast, is proposed to mediate receptor dimerization 16 and/or modulate the photoreactivity of LOV2. 14 Substitution of the conserved active-site cysteine with methionine has been shown to result in the formation of a unique photoproduct species absorbing maximally in the red region of the spectrum.…”

Section: Light-induced Activation Of Phot1mentioning

confidence: 99%

Phototropin Receptor Kinase Activation by Blue Light

Jones

Christie

2008

Plant Signaling & Behavior

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Phototropins (phot1 and phot2) are blue light-activated serine/ threonine protein kinases that function to mediate a variety of adaptive processes that serve to optimize the photosynthetic efficiency of plants and thereby promote their growth. Light sensing by the phototropins is mediated by a repeated motif located within the N-terminal region of the protein designated the LOV domain. Although phototropins possess two LOV photosensors (LOV1 and LOV2), recent biophysical and structure-function analyses clearly indicate that the LOV2 domain plays a predominant role in regulating phototropin kinase activity owing to specific protein changes that occur in response to LOV2 photoexcitation. In particular, the central b-sheet scaffold plays a role in propagating the photochemical signal generated from within LOV2 to protein changes at the surface that are necessary for kinase activation. Light-Induced Activation of Phot1The primary amino acid structures of plant phototropins (phot1 and phot2) can be separated into two distinct regions: a N-terminal photosensory region linked to a C-terminal effector domain that includes a classic serine/threonine kinase motif. [1][2][3] The N-terminal photosensory region comprises two LOV domains each of which binds the blue light absorbing cofactor flavin mononucleotide (FMN) as chromophore. 4,5 LOV domains exhibit significant homology to motifs found in a diverse range of eukaryotic and prokaryotic proteins involved in sensing Light, Oxygen or Voltage, hence the acronym LOV. 6 Bacterially expressed LOV domains are photochemically reactive as monitored by absorbance spectroscopy. 7 In the dark, LOV domains bind FMN non-covalently forming a spectral species, LOV 447 , which absorbs maximally near 447 nm. 7,8 Irradiation of the domain induces the formation of a covalent bond between the C(4a) carbon of the FMN and the sulfur atom of a nearby, conserved cysteine residue within the domain. Cysteinyl adduct formation occurs within microseconds of illumination and produces a spectral species, LOV 390 , that absorbs maximally near 390 nm. 8 Mutation of the afore-mentioned active-site cysteine to either alanine or serine results in a loss of photochemical reactivity of the LOV domain. 7,8 Moreover, this mutation has been used successfully to probe the roles of LOV1 and LOV2 in regulating phototropin activity and function. [9][10][11][12] As reported previously (ref. 13), the Cys → Ala mutation within LOV2 of Arabidopsis thaliana phot1 (C517A) results in a loss of light-induced receptor autophosphorylation when expressed in insect cells (Fig. 1A), demonstrating that LOV2 is the principle photosensor regulating phot1 kinase activity. A similar mode of action has been reported for the LOV2 domain of Arabidopsis phot2. 12,14,15 The LOV1 domain, by contrast, is proposed to mediate receptor dimerization 16 and/or modulate the photoreactivity of LOV2. 14 Substitution of the conserved active-site cysteine with methionine has been shown to result in the formation of a unique photoproduct species abso...

show abstract

Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain

Cited by 107 publications

References 15 publications

Structural Tuning of the Fluorescent Protein iLOV for Improved Photostability

Structural Tuning of the Fluorescent Protein iLOV for Improved Photostability

A chimeric photoreceptor gene, NEOCHROME, has arisen twice during plant evolution

Phototropin Receptor Kinase Activation by Blue Light

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