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PubMed2001

How do cyanobacteria sense and respond to light?

Cyanobacteria exhibit numerous responses to changes in the intensity and spectral quality of light. What sensors do cyanobacteria use to detect light and what are the mechanisms of signal transduction? The publication in 1996 of the complete genome sequence of the cyanobacterium Synechocystis 6803 provided a tremendous stimulus for research in this field, and many light-sensors and signal transducers have now been identified. However, our knowledge of cyanobacterial light-signal transduction remains fragmentary. This review summarizes what we know about the ways in which cyanobacteria perceive light, some of the ways which they respond to light signals and some recent achievements in elucidating the signal transduction mechanisms. Some problems in characterizing cyanobacterial signal transduction pathways are outlined and alternative experimental strategies are discussed.

Cyanobacteria↗
PubMedDate not supplied

Phototaxis in the cyanobacterium Synechocystis sp. PCC 6803: role of different photoreceptors.

The second cyanobacterial phytochrome Cph2 from Synechocystis sp. PCC 6803 was suggested as a part of a light-stimulated signal transduction chain inhibiting movement toward blue light. Cph2 has the two bilin binding sites, cysteine-129 and cysteine-1022, that might be involved in sensing of red/far-red and blue light, respectively. Here, we present data on wavelength dependence of the phototaxis inhibition under blue light, indicating that Cph2 itself is the photoreceptor for this blue light response. We found that inhibition of blue-light phototaxis in wild-type cells occurred below the transition point of about 470 nm. Substitution of cysteine-1022 with valine led to photomovement of the cells toward blue light (cph2(-) mutant phenotype). Analysis of mutants lacking cysteine-129 in the N-terminal chromophore binding domain indicated that this domain is also important for Cph2 function or folding of the protein. Furthermore, putative blue-light and phytochrome-like photoreceptors encoded by the Synechocystis sp. PCC 6803 genome were inactivated in wild-type and cph2 knockout mutant background. Our results suggest that none of these potential photoreceptors interfere with Cph2 function, although inactivation of taxD1 as well as slr1694 encoding a BLUF protein led to cells that reversed the direction of movement under blue light illumination in mutant strains of cph2.

Bacterial Proteins↗
PubMed2001

Direct reception of light by chromatophores of lower vertebrates.

Rapid color changes of lower vertebrates are caused by the motile activities of pigment cells (chromatophores) present in the skin tissue. Chromatophore motility is generally regulated by neural and/or by endocrine systems. However, in some cases, light also induces pigment aggregation or dispersion directly, which suggests the existence of visual pigments in chromatophores. In fact, some opsins, including melanopsin, have been identified. This article reviews light-sensitive chromatophores of lower vertebrates. Photoreceptive molecules (visual pigments) and signal transduction of light via a GTP-binding protein (G protein) are also discussed.

Animals↗
PubMed1998

Phytochrome-mediated light signals are transduced to nucleoside diphosphate kinase in Pisum sativum L. cv. Alaska.

To clarify the molecular mechanism for the transduction of light signals in plants, we have established an in vitro system that uses crude membrane and soluble fractions of stem sections of etiolated Pisum sativum L. cv. Alaska after irradiation by red light, or sequential application of red and far-red light to the stem section. In a previous report (T. Hamada et al., J. Photochem. Photobiol. B: Biol. 33 (1996) 143-151) the labelling of proteins in membrane fraction by [gamma-32P] ATP at 0 degree C for 15 s and subsequent separation of proteins by two-dimensional electrophoresis allowed unambiguous identification of a heavily phosphorylated protein spot at 18 kDa (p18). In the present study we have confirmed the former results in the membrane fraction, and obtained the result that an increase in the phosphorylation of p18 by red-light irradiation is observed in the soluble fraction. Further, we have provided evidence that the p18 in the soluble fraction is purified and identified as nucleoside diphosphate (NDP) kinase by Western blotting, immuno-precipitation, amino acid sequencing and cDNA analysis. Purified p18 shows autophosphorylation activity and strong phosphorylating activity against myelin basic protein (MBP), a substrate of MAP (mitogen activated protein) kinase. The results show that phytochrome-mediated light signals are transduced to NDP kinase, which may elicit signals by providing high concentrations of, for example, GTP from GDT and ATP, by the autophosphorylation and by the protein kinase activity similar to MAP kinase.

Alaska↗
PubMed1989

Arabidopsis thaliana mutant that develops as a light-grown plant in the absence of light.

The signal transduction pathways that lead to chloroplast biogenesis in plants are largely unknown. We describe here the identification and initial characterization of a novel genetic locus which fits the criteria of a regulatory gene located in a central pathway controlling light-mediated development. In the absence of light, these Arabidopsis thaliana mutants, designated det1 (de-etiolated 1), constitutively display many characteristics that are light-dependent in wild-type plants, including leaf and chloroplast development, anthocyanin accumulation, and accumulation of mRNAs for several light-regulated nuclear and chloroplast genes. The switch between dark and light growth modes thus appears to be a programmed step in a developmental pathway that is defined by det1. We suggest a model where the primary role of light on gene expression is mediated by the activation of leaf development. Further, the recessive nature of the det1 mutation implies that there is negative growth control on leaf development in dicotyledonous plants in the absence of light.

Anthocyanins↗
PubMed2001

[To see from light--biophysics of visual signal transduction].

To perform their functions within an organism, or to adapt to the environment as single cells, living cells react to signals detected by highly specialized receptor proteins. These include the G-protein coupled receptors (GPCRs), a receptor family, which comprises more than 1000 members, and is of outstanding significance in basic research and medical application. An archetype of a GPCR is the visual pigment rhodopsin, the photoreceptor of the retinal rod cell. Biophysical methods have largely contributed to the elucidation of rhodopsin structure and function, as well as of the corresponding signal cascade. This article discusses some of the more recent developments.

Animals↗
PubMed2005

Integration of light signaling with photoperiodic flowering and circadian rhythm.

Plants become photosynthetic through de-etiolation, a developmental process regulated by red/far-red light-absorbing phytochromes and blue/ultraviolet A light-absorbing cryptochromes. Genetic screens have identified in the last decade many far-red light signaling mutants and several red and blue light signaling mutants, suggesting the existence of distinct red, far-red, or blue light signaling pathways downstream of phytochromes and cryptochromes. However, genetic screens have also identified mutants with defective de-etiolation responses under multiple wavelengths. Thus, the optimal de-etiolation responses of a plant depend on coordination among the different light signaling pathways. This review intends to discuss several recently identified signaling components that have a potential role to integrate red, far-red, and blue light signalings. This review also highlights the recent discoveries on proteolytic degradation in the desensitization of light signal transmission, and the tight connection of light signaling with photoperiodic flowering and circadian rhythm. Studies on the controlling mechanisms of de-etiolation, photoperiodic flowering, and circadian rhythm have been the fascinating topics in Arabidopsis research. The knowledge obtained from Arabidopsis can be readily applied to food crops and ornamental species, and can be contributed to our general understanding of signal perception and transduction in all organisms.

Arabidopsis↗
PubMed2002

Signal transduction controlling the blue- and red-light mediated gene expression of S-adenosylmethionine decarboxylase in Pharbitis nil.

The signal transduction processes involved in the regulation of SAMDC gene expression by blue and red light were examined using pharmacological inhibitors of signalling pathways. Calcium and calmodulin positively regulated SAMDC gene expression in red light, whereas in blue light they regulated negatively. These results indicate that calcium homeostasis is involved in both red and blue light induction of SAMDC expression. Both signal transduction pathways also require new protein synthesis.

Adenosylmethionine Decarboxylase↗
PubMed1998

Gs alpha meets its target--shedding light on a key signal transduction event.

The recently determined crystal structure of Gs alpha bound to a catalytically active form of adenylyl cyclase reveals the location of the enzyme's active site and provides the first view of heterotrimeric G protein alpha subunit activating a downstream effector. Comparison with the structure of a catalytically inactive form of adenylyl cyclase suggests a plausible allosteric mechanism whereby the synergistic activators Gs alpha and forskolin stimulate the activity of adenylyl cyclase.

Adenosine Triphosphate↗
PubMed2002

Identification of a light-regulated protein kinase activity from seedlings of Arabidopsis thaliana.

Protein kinase transduction pathways are thought to be involved in light signaling in plants, but other than the photoreceptors, no protein kinase activity has been shown to be light-regulated in vivo. Using an in-gel protein kinase assay technique with histone H III SS as an exogenous substrate, we identified a light-regulated protein kinase activity with an apparent molecular weight ca 50 kDa. The kinase activity increased transiently after irradiation of dark-grown seedlings with continuous far red light (FR) and blue light (B) and decreased after irradiation with red light (R). The maximal activation was achieved after 30 min to 1 h with FR or B. After irradiation times longer than 2 h, the kinase activity decreased to below the sensitivity level of the assay. In Arabidopsis mutants lacking either the photoreceptors phytochrome A, phytochrome B or the blue-light receptor cryptochrome 1, kinase activity was undetectable, whereas in the photomorphogenic mutants cop1 and det1 the kinase activity was also observed in the absence of light signals, though still stimulated by B and FR. Interestingly, the R inhibition of the kinase activity was lost in the mutant hy5. Pretreatment with cycloheximide blocked the kinase activity.

Arabidopsis↗
PubMed1994

Arabidopsis mutants define downstream branches in the phototransduction pathway.

Light regulates the development of Arabidopsis seedlings in a variety of ways, including inhibition of hypocotyl growth and promotion of leaf development, chloroplast differentiation, and light-responsive gene expression. Mutations that uncouple most or all of these responses from light control have been described, for example, det1, det2, and cop1. To identify regulatory components that define downstream branches in the light-regulated signal transduction pathway, mutants specifically affected in only one light-regulated response were isolated. A screen was designed to isolate mutants that overexpressed the CAB (photosystem II type I chlorophyll a/b-binding proteins) genes in the dark, by use of transgenic line containing a T-DNA construct with two CAB3 promoter-reporter fusions. Eight mutants that showed aberrant expression of both CAB3 promoters were isolated and were designated doc mutants (for dark overepression of CAB). All of the mutants have normal etiolated morphology in the dark. Genetic and phenotypic analyses indicate that most of the mutations are recessive and define at least three loci (doc1, doc2, doc3). Unlike det1 and det2 mutants, which affect the expression of CAB and RBCS (the small subunit of RuBP carboxylase) to approximately the same extent, all three doc mutations are much more specific in derepressing the expression of CAB. The phenotypes of doc mutants suggest that morphological changes can be genetically separated from changes in CAB gene expression. Moreover, the regulation of CAB gene expression can be separated further from the regulation of RBCS gene expression. Epistasis studies suggest that DOC1 and DET3 act downstream from DET1 on two separate branches in the phototransduction pathway. In contrast, DOC2 appears to act on a distinct pathway from DET1. Mutations in doc1, doc2, or doc3 also impair plant growth under short-day conditions.

Arabidopsis↗
PubMed2005

Rhabdomeric phototransduction initiated by the vertebrate photopigment melanopsin.

Melanopsin is the photopigment that confers light sensitivity on intrinsically photosensitive retinal ganglion cells. Mammalian intrinsically photosensitive retinal ganglion cells are involved in the photic synchronization of circadian rhythms to the day-night cycle. Here, we report molecular components of melanopsin signaling using the cultured Xenopus dermal melanophore system. Photo-activated melanopsin is shown to initiate a phosphoinositide signaling pathway similar to that found in invertebrate photo-transduction. In melanophores, light increases the intracellular level of inositol trisphosphate and causes the dispersion of melanosomes. Inhibition of phospholipase C and protein kinase C and chelation of intracellular calcium block the effect of light on melanophores. At least four proteins, 43, 74, 90, and 134 kDa, are phosphorylated by protein kinase C upon light stimulation. This provides evidence of an invertebrate-like light-activated signaling cascade within vertebrate cells.

Animals↗
PubMed2002

The cyanobacterial phytochrome Cph2 inhibits phototaxis towards blue light.

We analysed the effects of inactivation of the phytochrome genes cph1 and cph2 on the phototactic migration of the cyanobacterium Synechocystis sp. PCC 6803 under different light qualities. Motility towards white, green, red and far red light was not altered in several independently raised cph1, cph2 and cph1/cph2 double mutants. Blue light (lambda = 400-500 nm) did not induce motility in wild-type and cph1 mutant cells, whereas cph2 and cph1/cph2 double mutants moved towards the blue light. Inhibition of the photosynthetic electron transport by DCMU influenced the motility of cph2 mutants under blue light, but not under white, red and far red light. RNA blot hybridizations did not indicate an altered transcript accumulation of the pilin-encoding pilA1 gene under blue light. We propose that the Cph2 protein is part of a light-stimulated signal transduction chain inhibiting the movement of Synechocystis sp. PCC 6803 cells towards blue light.

Bacterial Proteins↗
PubMed2006

[Blue light signaling in mosses].

Arabidopsis thaliana contains five identified blue light photoreceptors and at least one unidentified blue/UV-A light photoreceptor. Cryptochromes (CRY1 and CRY2) modulate photomorphological processes, flowering time, and circadian timing while phototrophins (PHOT1 and PHOT2) modulate phototropism, chloroplast movement, and stomatal opening. Flavins are the chromophores and absorb in the blue and UV-A range. Considerable information is known about the structure and mode of action of these photoreceptors. The moss Physcomitrella patens contains two identified cryptochromes (CRY1a and CRY1b) which modulate side branch formation and auxin metabolism. Blue light-induced chloroplast movement was mediated by four phototropins. Transduction of the blue/UV-A stimulus does involve calcium signaling in moss cells.

Bryophyta↗
PubMed2004

Blue light stimulates cyanobacterial motility via a cAMP signal transduction system.

The participation of cAMP in photosignal transduction in cyanobacteria was investigated. When cells of the cyanobacterium Synechocystis sp. PCC 6803 were exposed to light, cellular cAMP contents increased within a few minutes. Among incident monochromatic lights, blue light (450 nm) markedly increased cellular cAMP content, while red (630 nm) and far-red (720 nm) lights did not. Disruption of the cya1 gene encoding an adenylate cyclase caused the insensitivity of cellular cAMP level to blue light. Treatment of wild-type cells with the flavin antagonist phenylacetic acid inhibited this blue light effect. The motility of wild-type cells was enhanced by blue light, whereas that of cya1 mutant cells was not. Based on these results, we concluded that a blue light-cAMP signal transduction system stimulates the motility of Synechocystis sp. PCC 6803.

Adenylyl Cyclases↗
PubMed2006

Functional roles of the major chloroplast lipids in the violaxanthin cycle.

Monogalactosyldiacylglyceride (MGDG) and digalactosyldiacylglyceride (DGDG) are the major membrane lipids of chloroplasts. The question of the specialized functions of these unique lipids has received limited attention. One function is to support violaxanthin de-epoxidase (VDE) activity, an enzyme of the violaxanthin cycle. To understand better the properties of this system, the effects of galactolipids and phosphatidylcholines on VDE activity were examined by two independent methods. The results show that the micelle-forming lipid (MGDG) and bilayer forming lipids (DGDG and phosphatidylcholines) support VDE activity differently. MGDG supported rapid and complete de-epoxidation starting at a threshold lipid concentration (10 microM) coincident with complete solubilization of violaxanthin. In contrast, DGDG supported slow but nevertheless complete to nearly complete de-epoxidation at a lower lipid concentration (6.7 microM) that did not completely solubilize violaxanthin. Phosphotidylcholines showed similar effects as DGDG except that de-epoxidation was incomplete. Since VDE requires solubilized violaxanthin, aggregated violaxanthin in DGDG at low concentration must become solubilized as de-epoxidation proceeds. High lipid concentrations had lower activity possibly due to formation of multilayered structures (liposomes) that restrict accessibility of violaxanthin to VDE. MGDG micelles do not present such restrictions. The results indicate VDE operates throughout the lipid phase of the single bilayer thylakoid membrane and is not limited to putative MGDG micelle domains. Additionally, the results also explain the differential partitioning of violaxanthin between the envelope and thylakoid as due to the relative solubilities of violaxanthin and zeaxanthin in MGDG, DGDG and phospholipids. The violaxanthin cycle is hypothesized to be a linked system of the thylakoid and envelope for signal transduction of light stress.

Chloroplasts↗
PubMed2003

The LOV domain family: photoresponsive signaling modules coupled to diverse output domains.

For single-cell and multicellular systems to survive, they must accurately sense and respond to their cellular and extracellular environment. Light is a nearly ubiquitous environmental factor, and many species have evolved the capability to respond to this extracellular stimulus. Numerous photoreceptors underlie the activation of light-sensitive signal transduction cascades controlling these responses. Here, we review the properties of the light, oxygen, or voltage (LOV) family of blue-light photoreceptor domains, a subset of the Per-ARNT-Sim (PAS) superfamily. These flavin-binding domains, first identified in the higher-plant phototropins, are now shown to be present in plants, fungi, and bacteria. Notably, LOV domains are coupled to a wide array of other domains, including kinases, phosphodiesterases, F-box domains, STAS domains, and zinc fingers, which suggests that the absorption of blue light by LOV domains regulates the activity of these structurally and functionally diverse domains. LOV domains contain a conserved molecular volume extending from the flavin cofactor, which is the locus for light-driven structural change, to the molecular surface. We discuss the role of this conserved volume of structure in LOV-regulated processes.

Amino Acid Sequence↗