Fresh view of light signal transduction in plants.
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Darkness↗
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UV-B, UV-A, and blue light signal transduction pathways interact synergistically to regulate chalcone synthase gene expression in Arabidopsis.
UV and blue light stimulate transcription of key flavonoid biosynthesis genes in a range of higher plants. Here, we provide evidence that several distinct "inductive" and "synergistic" UV/blue phototransduction pathways regulate chalcone synthase (CHS) gene transcription and transcript accumulation in Arabidopsis leaf tissue. Experiments with the long-hypocotyl hy4-2.23N mutant showed that separate inductive pathways mediate responses to UV-B and UV-A/blue light. Only the UV-A/blue light induction of CHS expression involved the CRY1 photoreceptor. In addition, UV-A and blue light each act synergistically with UV-B to stimulate CHS transcript accumulation and beta-glucuronidase activity driven by a CHS promoter in transgenic leaf tissue. The UV-A and blue phototransduction pathways responsible for synergism are distinct because they produce transient and relatively stable signals, respectively, and can function additively to stimulate CHS promoter function. The hy4-2.23N mutant retains the synergistic interactions between UV-B and both UV-A and blue light, indicating that neither synergism pathway involves the CRY1 photoreceptor. Our findings reveal considerable complexity in both photoreception and signal transduction in regulating CHS gene expression by UV and blue light.
Acyltransferases↗
[Phytochrome and light signal transduction].
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Arabidopsis↗
Functional analysis of EID1, an F-box protein involved in phytochrome A-dependent light signal transduction.
Empfindlicher im Dunkelroten Licht 1 (EID1) is an F-box protein that functions as a negative regulator in phytochrome A (phyA)-specific light signalling. F-box proteins are components of SCF ubiquitin ligase complexes that target proteins for degradation in the proteasome. Here we present further characterization of EID1 at the expression level, and show that it regulates photomorphogenesis in seedlings, rosette leaf development and flowering. Data on transcript expression patterns indicate that EID1 is expressed during all stages of Arabidopsis development and exhibits no light response. Microscope studies demonstrate that EID1 is localized to the nucleus, where it can form speckles under continuous far-red light that resemble clastosomes. To characterize the composition and formation of SCF(EID1) complexes further, we used two-hybrid and bridge assays in yeast and in planta. EID1 interacts specifically with several Arabidopsis Skp1-like (ASK) proteins and Cullin1 to form stable dimeric and trimeric complexes. Our results support a two-step association process in which the F-box protein binds first to the ASK adaptor, forming a unit which then associates with the catalytic core of the SCF complex. Finally, our data indicate that the EID1 target interaction domain is composed of two independent modules.
Alleles↗
Let there be light: signal transduction in a mammalian circadian system.
Mammalian circadian rhythms are controlled by a biological clock located in the hypothalamic suprachiasmatic nuclei (SCN). This clock is entrained by light through a retinohypothalamic pathway that interacts with the SCN through glutamate neurotransmission. Light pulses during the subjective night induce phase shifts of behavioral rhythms, and also trigger intracellular changes such as the expression of immediate-early genes and activation of transcription factors. In this review, we present a model of the signal transduction pathway leading to photic synchronization of the circadian clock, including the activity of specific second messenger systems, gene expression, and interaction between potential agents capable of producing phase shifts.
Animals↗
Role of a white collar-1-white collar-2 complex in blue-light signal transduction.
Mutations in either white collar-1 (wc-1) or white collar-2 (wc-2) lead to a loss of most blue-light-induced phenomena in Neurospora crassa. Sequence analysis and in vitro experiments show that WC-1 and WC-2 are transcription factors regulating the expression of light-induced genes. The WC proteins form homo- and heterodimers in vitro; this interaction could represent a fundamental step in the control of their activity. We demonstrate in vivo that the WC proteins are assembled in a white collar complex (WCC) and that WC-1 undergoes a change in mobility due to light-induced phosphorylation events. The phosphorylation level increases progressively upon light exposure, producing a hyperphosphorylated form that is degraded and apparently replaced in the complex by a newly synthesized WC-1. WC-2 is unmodified and also does not change quantitatively in the time frame examined. Light-dependent phosphorylation of WC-1 also occurs in a wc-2 mutant, suggesting that a functional WC-2 is dispensable for this light-specific event. These results suggest that light-induced phosphorylation and degradation of WC-1 could play a role in the transient expression of blue-light-regulated genes. Our findings suggest a mechanism by which WC-1 and WC-2 mediate light responses in Neurospora.
Animals↗
KIDARI, encoding a non-DNA Binding bHLH protein, represses light signal transduction in Arabidopsis thaliana.
Through activation tagging mutagenesis, we isolated a kidari-D (kdr-D) mutant, which exhibited a defect in blue and far-red light mediated photomorphogenesis. Under continuous blue light, the kdr-D mutant showed long hypocotyl phenotype, whereas it showed normal cotyledon opening and expansion. In addition, the kdr-D showed slightly longer hypocotyl under continuous far-red light, suggesting that KDR functions in a branch of cry signaling and mediates a cross-talk between cry and phyA. In the kdr-D mutant, a gene encoding a putative basic/Helix-Loop-Helix (bHLH) protein was overexpressed by the insertion of 35S enhancer into 10 kb upstream of the gene. Consistently, overexpression of this gene recapitulated the phenotype of kdr-D. KDR is composed of 94 amino acids with non-DNA binding HLH domain, a structure found in human Inhibitor of DNA binding 1 (Id-1) which functions as a negative regulator of bHLH proteins through heterodimerization with them. The KDR specifically interacted with HFR1, a bHLH protein regulating photomorphogenesis, in yeast two hybrid assay and the kdr-D was epistatic to 35S::HFR1 in the hypocotyl phenotype. Thus, it shows that KDR functions as a negative regulator of HFR1, similar to Id-1 in human. The KDR exhibited circadian expression pattern with an increase during the day. Taken together, our results suggest that KDR attenuates light mediated responses in day light condition through inhibition of the activity of bHLH proteins involved in light signaling.
Amino Acid Sequence↗
Seeing the light: news in Neurospora blue light signal transduction.
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Adaptation, Physiological↗
Genetic analysis of signal transduction through light-induced protein phosphorylation in Neurospora crassa perithecia.
We have previously demonstrated that blue light induces the phosphorylation of a 15-kDa protein in crude membrane fractions of Neurospora crassa mycelia. Here we report the isolation and characterization of a mutant (psp; phosphorylation of small proteins that is completely defective for phosphorylation of that protein, as assayed in both crude membrane and soluble fractions. This mutation defines a unique locus that maps to linkage group VR between al-3 and his-6. To elucidate the photobiological significance of the phosphorylation of the protein, we analyzed known photobiological phenomena and discovered that the positioning of beaks on the perithecia, defined as perithecial polarity, was light-dependent in the wild type. In the psp mutant, beaks were phototropic as in the wild type, but their position was random. In a wc-l mutant, however, beaks were positioned at random and were not phototropic. Thus light-induced perithecial polarity and phototropism of perithecial beaks are controlled differently. A psp; wc-l double mutant showed the same phenotype as that of wc-l with respect to these two photomorphogenetic characters. These results indicate that the wc-l gene is epistatic to psp in the light-signal transduction pathway that controls both phototropism and perithecial polarity.
DNA-Binding Proteins↗
Photic regulation of melatonin in humans: ocular and neural signal transduction.
Light is a potent stimulus for regulating the pineal gland's production of melatonin and the broader circadian system in humans. It initially was thought that only very bright photic stimuli (> or = 2500 lux) could suppress nocturnal melatonin secretion and induce other circadian responses. It is now known that markedly lower illuminances (< or = 200 lux) can acutely suppress melatonin or entrain and phase shift melatonin rhythms when exposure conditions are optimized. The elements for physical/biological stimulus processing that regulate photic influences on melatonin secretion include the physics of the light source, gaze behavior relative to the light source, and the transduction of light energy through the pupil and ocular media. Elements for sensory/neural signal processing become involved as photons are absorbed by retinal photopigments and neural signals are generated in the retinohypothalamic tract. Aspects of this physiology include the ability of the circadian system to integrate photic stimuli spatially and temporally as well as the wavelength sensitivity of the operative photoreceptors. Acute, light-induced suppression of melatonin is proving to be a powerful tool for clarifying how these elements of ocular and neural physiology influence the interaction between light and the secretion of melatonin from the human pineal gland.
Animals↗
Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction.
Proteins containing a sensor of blue light using FAD (BLUF) domain control diverse cellular processes, such as gene expression, nucleotide metabolism and motility, by relaying blue light signals to distinct output units. Despite its crucial and widespread functions, the mechanism of BLUF signal transduction has remained elusive. We determined crystal structures of the dark-adapted state and of a photo-excited, red-shifted photocycle intermediate of the BLUF unit of AppA, a purple bacterial photoreceptor involved in the light-dependent regulation of photosynthesis gene expression. In contrast to a recently published crystal structure of the AppA BLUF domain determined in the presence of detergent molecules, our structural model of the dark state corresponds well to those reported for the BLUF domains of Tll0078 and BlrB. This establishes that a highly conserved methionine (Met106 in AppA) is next to the active site glutamine (Gln63 in AppA), which is of relevance for the latter's orientation in the dark state and for the mechanism of the photoreaction. The comparison of the dark-adapted and photointermediate state structures shows light-induced conformational alterations, which suggest a path for signal propagation. In particular, we observe a significant movement of the Met106 side-chain. Met106 thereby changes its mode of interaction with Gln63, which supports a light-dependent rotation of the latter. In view of other BLUF structures available, our data further suggest that the hydrogen bond between Asn45 and the backbone carbonyl of His105 breaks upon illumination. The ensuing extensive structural rearrangement of beta-strand 5 is predicted to involve a flip of Met106 out of the flavin-binding pocket and Trp104 moving in to fill the void. We propose that the blue light signal is transmitted towards the surface of the BLUF domain via His44, which serves as a reporter of active site changes.
Bacterial Proteins↗
Photoreceptors of the retina and pinealocytes of the pineal gland share common components of signal transduction.
Light absorbed by retinal photoreceptors triggers a cascade of reactions that initiate cGMP hydrolysis, cation channel closure and membrane hyperpolarization. Down-regulation of the cascade involves additional proteins that interfere with amplification along the cascade. Pinealocytes are activated by norepinephrine during the dark phase of the day/night cycle. Mature pinealocytes of the mammalian pineal express the known photoreceptor proteins that are implicated in down-regulation of the visual cascade, but the cascade components that produce cGMP hydrolysis and membrane hyperpolarization are absent. Pinealocytes accumulate cyclic AMP minimally when norepinephrine activates their beta adrenergic receptors alone, but the response is potentiated by the simultaneous activation of their alpha-1 adrenergic receptors. A model is proposed whereby phosducin, a phosphoprotein that binds the beta,gamma subunit of G-proteins, could modulate the synthesis of cyclic AMP by buffering the amount of beta,gamma G-protein subunits that are available for activating adenylate cyclase.
Animals↗
White collar proteins: PASsing the light signal in Neurospora crassa.
The filamentous fungus Neurospora crassa is an excellent paradigm for the study of blue light signal transduction. The isolation and characterization of the genes for two central regulators of the blue light response, white collar-1 and white collar-2, have begun to shed light on the mechanism of blue light signal transduction in fungi. These proteins are not only proposed to encode blue-light-activated transcription factors but also to be elements of the blue light signal transduction pathway.
Circadian Rhythm↗
Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction.
Phototropin, a major blue-light receptor for phototropism in seed plants, exhibits blue-light-dependent autophosphorylation and contains two light, oxygen, or voltage (LOV) domains and a serine/threonine kinase domain. The LOV domains share homology with the PER-ARNT-SIM (PAS) superfamily, a diverse group of sensor proteins. Each LOV domain noncovalently binds a single FMN molecule and exhibits reversible photochemistry in vitro when expressed separately or in tandem. We have determined the crystal structure of the LOV2 domain from the phototropin segment of the chimeric fern photoreceptor phy3 to 2.7-A resolution. The structure constitutes an FMN-binding fold that reveals how the flavin cofactor is embedded in the protein. The single LOV2 cysteine residue is located 4.2 A from flavin atom C(4a), consistent with a model in which absorption of blue light induces formation of a covalent cysteinyl-C(4a) adduct. Residues that interact with FMN in the phototropin segment of the chimeric fern photoreceptor (phy3) LOV2 are conserved in LOV domains from phototropin of other plant species and from three proteins involved in the regulation of circadian rhythms in Arabidopsis and Neurospora. This conservation suggests that these domains exhibit the same overall fold and share a common mechanism for flavin binding and light-induced signaling.
Amino Acid Sequence↗
RED1 is necessary for phytochrome B-mediated red light-specific signal transduction in Arabidopsis.
Seedlings of a transgenic Arabidopsis line (ABO) that overexpresses phytochrome B (phyB) display enhanced deetiolation specifically in red light. To identify genetic loci necessary for phytochrome signal transduction in red light, we chemically mutagenized ABO seeds and screened M2 seedlings for revertants of the enhanced deetiolation response. One recessive, red light-specific extragenic revertant, designated red1, was isolated. The mutant phenotype was expressed in the original ABO background as well as in the nontransgenic Nossen (No-0) progenitor background. red1 is also deficient in several other aspects of red light-induced responses known to be mediated by phyB, such as inhibition of petiole elongation and the shade avoidance response. red1 was mapped to the bottom of chromosome 4 at a position distinct from all known photoreceptor loci. Together with complementation analysis, the data show that red1 is a novel photomorphogenic mutant. The evidence suggests that red1 represents a putative phytochrome signal transduction mutant potentially specific to the phyB pathway.
Arabidopsis↗
Active oxygen species in blue light mediated signal transduction in coleoptile tips.
Coleoptile tip is a blue-light sensitive tissue possessing a "blue light receptor" which, upon activation, elicits a signal cascade resulting in phototropic curvature of the coleoptile. In this context, the nature of the photoreceptors and the exact mechanism through which the photoreceptors transduces the signal across the membrane are not clear. In this study, we attempted to examine whether the blue light receptor perturbs redox status of the coleoptile tip and sensitizes molecular oxygen as part of the signal reactions. Coleoptile tips of Sorghum bicolor and wheat (Triticum vulgare) grown in the dark showed pronounced ascorbate free radical signal, which diminished upon illumination with weak blue light for one minute. Concomitantly, the generation of superoxide radical by the coleoptile tip was augmented upon illumination with blue light. Various thiol blockers tested in this study caused powerful inhibition of blue light induced superoxide anion radical generation. Treatment with these thiol blockers, with the exception of NEM, resulted in marked increase in the levels of ascorbic acid free radical in the blue light irradiated coleoptiles. The blue light stimulated O*-2-generation by the coleoptile tip homogenate is also inhibited by the inhibitors of blue light responses viz phenylacetic acid, potassium iodide, and sodium azide. Based on our observations, we postulate that the activated blue light receptor present in the coleoptile tip sensitizes molecular oxygen to superoxide anion radical in the tip initializing the blue light signal cascade reactions.
Ascorbic Acid↗
Intracellular trafficking of photoreceptors during light-induced signal transduction in plants.
Plants monitor changes in the ambient light environment by highly specialised photoreceptors, which include the red/far-red photoreversible phytochromes, the blue-light-absorbing cryptochromes and phototropin and the so-far-unidentified UVB photoreceptor(s). Light easily penetrates plant organs/tissues and reaches even the subcellular compartments of various cell types. Therefore, it is not surprising that the determination of the intracellular localisation of photoreceptors has been, for many years, a major, and often controversial, subject of plant photobiology and cell biology research. Phototropin, one of the blue-light photoreceptors of higher plants, controls phototropism by monitoring the direction of light, and it is localised in or at the plasmalemma. In contrast, the subcellular localisation of phytochromes changes dynamically and exhibits a very complex pattern. These photoreceptors are localised in the cytosol in dark- grown tissues. Irradiation, however, induces import of phytochromes into the nucleus. The import occurs in a light-quality- and light-quantity-dependent fashion and, as such, seems to be unique to higher plants. Light-induced accumulation of phytochromes in the nuclei correlates well with various physiological responses mediated by these photoreceptors. These observations indicate that light-dependent intracellular redistribution of phytochrome photoreceptors is one of the major regulatory steps in photomorphogenesis.
Darkness↗
Arabidopsis contains at least four independent blue-light-activated signal transduction pathways.
We have investigated the stomatal and phototropic responses to blue light of a number of single and double mutants at various loci that encode proteins involved in blue-light responses in Arabidopsis. The stomatal responses of light-grown mutant plants (cry1, cry2, nph1, nph3, nph4, cry1cry2, and nph1cry1) did not differ significantly from those of their wild-type counterparts. Second positive phototropic responses of etiolated mutant seedlings, cry1, cry2, cry1cry2, and npq1-2, were also similar to those of their wild-type counterparts. Although npq1 and single and double cry1cry2 mutants showed somewhat reduced amplitude for first positive phototropism, threshold, peak, and saturation fluence values for first positive phototropic responses of etiolated seedlings did not differ from those of wild-type seedlings. Similar to the cry1cry2 double mutants and to npq1-2, a phyAphyB mutant showed reduced curvature but no change in the position or shape of the fluence-response curve. By contrast, the phototropism mutant nph1-5 failed to show phototropic curvature under any of the irradiation conditions used in the present study. We conclude that the chromoproteins cry1, cry2, nph1, and the blue-light photoreceptor for the stomatal response are genetically separable. Moreover, these photoreceptors appear to activate separate signal transduction pathways.
Arabidopsis↗