Abstract:Flagellate green algae such as Chlamydomonas and related genera are guided by their eyes to places where light conditions are optimal for photosynthetic growth. These eyes constitute the simplest and most common visual system found in nature. The eyes contain optics, photoreceptors and the elementary components of a signal-transduction chain. Rhodopsin serves as the photoreceptor, as it does in animal vision. Upon light stimulation, its all-trans-retinal chromophore isomerizes into 13-cis and activates a photo… Show more
“…Chlamydomonas , the all-transretinal polyene chromophore isomerizes upon light stimulation to 13-cis and activates a photoreceptor channel, leading to a rapid Ca 2 + influx into the eyespot region. The Ca 2 + fluxes represent the molecular basis for phototaxis (Hagemann, 1997). Recently, a new type of rhodopsin, channelrhodopsin, has been reported from Chlamydomonas reinhardtii .…”
b -apo-carotenals as well as apo-lycopenals into retinal, (3R)-3-hydroxy-retinal and acycloretinal respectively. In addition, the alcohols of these substrates were cleaved to yield the corresponding retinal derivatives.
“…Chlamydomonas , the all-transretinal polyene chromophore isomerizes upon light stimulation to 13-cis and activates a photoreceptor channel, leading to a rapid Ca 2 + influx into the eyespot region. The Ca 2 + fluxes represent the molecular basis for phototaxis (Hagemann, 1997). Recently, a new type of rhodopsin, channelrhodopsin, has been reported from Chlamydomonas reinhardtii .…”
b -apo-carotenals as well as apo-lycopenals into retinal, (3R)-3-hydroxy-retinal and acycloretinal respectively. In addition, the alcohols of these substrates were cleaved to yield the corresponding retinal derivatives.
“…Recently, anomalous concentrations of RAs and 4-oxoRAs (up to 20 ng/L) were measured in some protected drinking water sources (30), which suggested that there might be unidentified sources of RAs in aquatic systems. There are some reports on the existence of retinal, one of the precursors of RAs, in algae, and isomerization of the all-trans-retinal chromophore into 13-cis-retinal activated the photoreceptor channel, whereas RAs were not associated with photoreceptors in algae (31)(32)(33). The nonanimal hydroxylase enzyme (CYP120A1) in the cyanobacteria Synechocystis was reported to be capable of converting RAs to corresponding hydroxyl derivatives (34), and a hydroxylated RA, 7-OH-RA, has recently been observed in several species of cyanobacteria (35).…”
Deformed amphibians have been observed in eutrophic habitats, and some clues point to the retinoic acids (RAs) or RA mimics. However, RAs are generally thought of as vertebrate-specific hormones, and there was no evidence that RAs exist in cyanobacteria or algae blooms. By analyzing RAs and their analogs 4-oxo-RAs in natural cyanobacteria blooms and cultures of cyanobacteria and algae, we showed that cyanobacteria blooms could produce RAs, which were powerful animal teratogens. Intracellular RAs and 4-oxo-RAs with concentrations between 0.4 and 4.2 × 10 2 ng/L were detected in all bloom materials, and extracellular concentrations measured in water from Taihu Lake, China, were as great as 2.0 × 10 ng/L, which might pose a risk to wildlife through chronic exposure. Further examination of 39 cyanobacteria and algae species revealed that 32 species could produce RAs and 4-oxo-RAs (1.6-1.4 × 10 3 ng/g dry weight), and the dominant cyanobacteria species in Taihu Lake, Microcystis flos-aquae and Microcystis aeruginosa, produced high amounts of RAs and 4-oxo-RAs with concentrations of 1.4 × 10 3 and 3.7 × 10 2 ng/g dry weight, respectively. Most genera of cyanobacteria that could produce RAs and 4-oxo-RAs, such as Microcystis, Anabaena, and Aphanizomenon, often occur dominantly in blooms. Production of RAs and 4-oxo-RAs by cyanobacteria was associated with species, origin location, and growth stage. These results represent a conclusive demonstration of endogenous production of RAs in freshwater cyanobacteria blooms. The observation of teratogenic RAs in cyanobacteria is evolutionarily and ecologically significant because RAs are vertebrate-specific hormones, and cyanobacteria form extensive and highly visible blooms in many aquatic ecosystems.eutrophication | phytoplankton | deformities | Asia
“…Fitting with a sum of two saturating functions reveals a slower low-light-saturating current and faster high-light-saturating current (9-11, 16, 17), which were interpreted as being driven by either a single, or two different, photoreceptor proteins (18). Multiple photoreceptors have been considered, based on the complex shape of the photoreceptorcurrent action spectrum (8,11,14), and results from retinalreconstitution studies (19).For several years the most abundant protein in the eyespot membranes of Chlamydomonas and Volvox has been considered as the photoreceptor for photomotile responses in these algae (20,21). However, recently the so-called ''chlamyrhodopsin'' (21) has been ruled out as the photoreceptor pigment for either phototaxis or the photophobic response in Chlamydomonas (22).…”
We demonstrate that two rhodopsins, identified from cDNA sequences, function as low-and high-light-intensity phototaxis receptors in the eukaryotic alga Chlamydomonas reinhardtii. Each of the receptors consists of an Ϸ300-residue seven-transmembrane helix domain with a retinal-binding pocket homologous to that of archaeal rhodopsins, followed by Ϸ400 residues of additional membraneassociated portion. The function of the two rhodopsins, Chlamydomonas sensory rhodopsins A and B (CSRA and CSRB), as phototaxis receptors is demonstrated by in vivo analysis of photoreceptor electrical currents and motility responses in transformants with RNA interference (RNAi) directed against each of the rhodopsin genes. The kinetics, fluence dependencies, and action spectra of the photoreceptor currents differ greatly in transformants in accord with the relative amounts of photoreceptor pigments expressed. The data show that CSRA has an absorption maximum near 510 nm and mediates a fast photoreceptor current that saturates at high light intensity. In contrast, CSRB absorbs maximally at 470 nm and generates a slow photoreceptor current saturating at low light intensity. The relative wavelength dependence of CSRA and CSRB activity in producing phototaxis responses matches precisely the wavelength dependence of the CSRA-and CSRB-generated currents, demonstrating that each receptor mediates phototaxis. The saturation of the two photoreceptor currents at different light fluence levels extends the range of light intensity to which the organism can respond. Further, at intensities where both operate, their light signals are integrated at the level of membrane depolarization caused by the two photoreceptor currents.retinal protein ͉ photoreceptor ͉ receptor currents ͉ signal transduction U nicellular flagellate algae optimize their light environment by motility responses. Phototaxis (or oriented movement) guides them toward or away from a light source, whereas photophobic responses prevent their crossing a light͞dark border (1). In Chlamydomonas reinhardtii these photomotility responses are mediated by retinal-containing receptor(s), as shown by retinal reconstitution studies in blind mutants (2-5). Moreover, it has been established that the native chromophore of the photoreceptor protein(s) is 6-s-trans all-trans-retinal, as in archaeal rhodopsins, and its alltrans͞13-cis isomerization is required for triggering behavioral responses (3,4,6).A complex photoreceptor apparatus is used to track the light source. The photoreceptor molecules appear to be localized in a small portion of the plasma membrane overlying the eyespot. Light absorption͞reflection by the eyespot modulates the photoreceptor illumination during helical swimming if the helix axis does not coincide with the light direction (7). This modulated illumination serves as a signal for the correction of the swimming path.A cascade of electrical phenomena plays a key role in the signal transduction. Photoexcitation of the receptor molecules results in the generation of photoreceptor...
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