Afterpotentials in dronefly retinula cells

Summary The wavelength dependence of the afterpotentials following a bright illumination was studied in single photoreceptor cells of the droneflyEristalis. Cells with only a spectral sensitivity peak in the blue were selected. As previously demonstrated, these cells contain a rhodopsin absorbing maximally at about 450–460 nm, which upon photoconversion transforms into a metarhodopsin absorbing maximally at about 550 nm (Tsukahara and Horridge, 1977).With the visual pigment initially all in the rhodopsin form, a high rate of visual pigment conversion results in an afterhyperpolarization (AHP) when the fraction of metarhodopsin remains negligible after illumination as occurs at longer wavelengths if the intensity is high. Intensive illumination at short wavelengths is followed by a prolonged depolarizing afterpotential (PDA). The magnitude of the PDA peaks at low intensities at about 450–460 nm, corresponding to the peak of the cell's spectral sensitivity (i.e. the rhodopsin peak). With increasing intensity of illumination, however, the peak shifts progressively towards 430 nm, which corresponds to the photoequilibrium with maximum metarhodopsin that can be established by monochromatic light. From this result, it is inferred that the PDA is related to the induced fall in the rhodopsin fraction. The PDA can be abolished, or knocked down, by a long-wavelength flash which reconverts remaining metarhodopsin into rhodopsin. Therefore the decline of the PDA is restrained by the existing amount of metarhodopsin. Possible theories of afterpotentials are discussed.     

The ultrastructure of the uterine epithelium of the pig during the estrous cycle and early pregnancy

Summary In the compound eye of the moth Antheraea polyphemus, three types of visual pigments were found in extracts from the retina and by microspectrophotometry in situ. The absorption maxima of the receptor pigment P and the metarhodopsin M are at (1) P 520–530 nm, M 480–490 nm; (2) P 460–480 nm, M 530–540 nm; (3) P 330–340 nm, M 460–470 nm. Their localization was investigated by electron microscopy on eyes illuminated with different monochromatic lights. Within the tiered rhabdom, constituted of the rhabdomeres of nine visual cells, the basal cell contains a blue-and the six medial cells have a greenabsorbing pigment. The two distal cells of most ommatidia also have the blue pigment; only in the dorsal region of the eye, these cells contain a UV-absorbing pigment, which constitutes a portion of only 5% of the visual pigment content within the entire retina. The functional significance of this distribution is discussed.     

Reversible phosphorylation of opsin induced by irradiation of blowfly retinae

Summary Light-induced phosphorylation and dephosphorylation of the visual pigment protein, opsin, was investigated in isolated retinae of the blowfly making use of the fact that photon capture by rhodopsin leads to the formation of a thermostable metarhodopsin. Retinae were exposed, in the presence of exogenous³²P-orthophosphate, to an intense blue light which initiated the phosphorylation of opsin (half-time about 5 min at 25 °C). Subsequent exposure of the retina to red light converted all the metarhodopsin present into rhodopsin and triggered a relatively rapid dephosphorylation of rhodopsin (half-time less than 20 s). It is proposed that the phosphorylated forms of rhodopsin and metarhodopsin represent inactive states of the pigment, i.e. phosphorylated metarhodopsin does not initiate reactions leading to the excitation of the photoreceptor cell and phosphorylated rhodopsin cannot be converted into physiologically active metarhodopsin without first being dephosphorylated.Abbreviations R1–6 peripheral retinula cells of the blowfly ommatidium - PDA prolonged depolarizing afterpotential - R rhodopsin - M metarhodopsin - R-P _n phosphorylated rhodopsin - M-P _n phosphorylated metarhodopsin - SDS-PAGE sodium dodecylsulphate polyacrylamide gel electrophoresis     

Dark adaptation,sensitivity, and rhodopsin level in the eye of the lobster,Homarus

Summary Dark adaptation of living lobsters was measured by recording the ERG at several temperatures in the range 5–20 °C following adapting flashes that convert about 70% of the rhodopsin to metarhodopsin. Recovery of log threshold is rapid, and at 10–20° is nearly complete in 10 min. Only at 5 °C is dark adaptation significantly slowed. Comparison of dark adaptation with data on regeneration of pigment (Bruno et al., 1977) is consistent with the hypothesis that as rhodopsin concentration rises and falls, its only effect on sensitivity is to alter the probability of quantum catch. This interpretation is further bolstered by observations on winter lobsters that have a 70% deficiency of rhodopsin without the concomitant increase in metarhodopsin that accompanies light adaptation. No effect of metarhodopsin on sensitivity was detected. These experiments support the growing body of evidence indicating that the relationship between rhodopsin concentration and log threshold is fundamentally different in the rhabdomeric photoreceptors of invertebrates and the rods and cones of vertebrates.This work was supported by USPHS research grant EY 00222 to Yale University. S.N.B. was aided by NIH Postdoctoral Fellowship EY 52378, by funds made available through the Unidel Foundation, and by a grant from the University of Delaware Research Foundation.     

Spectral absorption and sensitivity measurements in single ommatidia of the green crab,Carcinus

Summary Rhabdoms of the green crabCarcinus maenas were examined by microspectrophotometry and found to contain a visual pigment with _max at 502–506 nm. Upon irradiation, a stable metarhodopsin formed with unchanged _max and molar extinction coefficient. In the presence of 5% glutaraldehyde the rhabdoms were photobleached. Partial bleaching experiments indicate that in the rhabdoms studied, only one visual pigment was present, with an absorption spectrum appropriate for a hypothetical rhodopsin from Dartnall's (1953) nomogram.Retinular (photoreceptor) cells were studied with microelectrodes. They had negative resting potentials of 30–65 mV and responded to light with depolarizing receptor potentials. All cells had maximum sensitivity at ~493 nm, as did the ERG (electroretinogram). Selective adaptation failed to alter the spectral sensitivity functions of single cells or the ERG. If these spectral sensitivity data are pooled with Wald's (1968), the average sensitivity of the dark-adapted eye is accounted for adequately by the pigment of the rhabdom.The results of this work do not support the hypothesis of Horridge (1967) that each ommatidium ofCarcinus has two color receptors.This work was supported by U.S. P.H.S. grant EY 00222.     

Studies of fluorescence inDrosophila compound eyes: changes induced by intense light and vitamin A deprivation

Summary Ultraviolet light excites a red fluorescence fromDrosophila R1–6 rhabdomeres which is superimposed on a blue background emission. Metarhodopsin (M570) pigment generates some or all of the vitamin A dependent red emission. However, the excitation spectrum for red emission peaks in the UV. This suggests that the pigment which sensitizes R1–6's visual pigment to UV light (sensitizing pigment) absorbs the UV light, sensitizing metarhodopsin's fluorescence by energy transfer. Blue emission is neither from sensitizing pigment nor from visual pigment as shown by vitamin A deprivation studies.Very intense UV or blue stimulation causes these changes: (1) conversion of visual pigment into a fluorescent product; (2) destruction of this fluorescent product; (3) a decrease in the blue background fluorescence (even in vitamin A deprived flies); and (4) a permanent destruction of visual pigment and retinal degeneration. The first effect requires intensities 3 log units brighter than needed to interconvert rhodopsin and metarhodopsin 1/2 way to photoequilibrium. UV light is about 5 times as effective as blue light for the conversion of visual pigment into fluorescent product.     

Metarhodopsin control by arrestin,light-filtering screening pigments,and visual pigment turnover in invertebrate microvillar photoreceptors

The visual pigments of most invertebrate photoreceptors have two thermostable photo-interconvertible states, the ground state rhodopsin and photo-activated metarhodopsin, which triggers the phototransduction cascade until it binds arrestin. The ratio of the two states in photoequilibrium is determined by their absorbance spectra and the effective spectral distribution of illumination. Calculations indicate that metarhodopsin levels in fly photoreceptors are maintained below ~35% in normal diurnal environments, due to the combination of a blue-green rhodopsin, an orange-absorbing metarhodopsin and red transparent screening pigments. Slow metarhodopsin degradation and rhodopsin regeneration processes further subserve visual pigment maintenance. In most insect eyes, where the majority of photoreceptors have green-absorbing rhodopsins and blue-absorbing metarhodopsins, natural illuminants are predicted to create metarhodopsin levels greater than 60% at high intensities. However, fast metarhodopsin decay and rhodopsin regeneration also play an important role in controlling metarhodopsin in green receptors, resulting in a high rhodopsin content at low light intensities and a reduced overall visual pigment content in bright light. A simple model for the visual pigment–arrestin cycle is used to illustrate the dependence of the visual pigment population states on light intensity, arrestin levels and pigment turnover.     

Localization of visual pigments within rhabdoms of the compound eye of Spodoptera exempta (Insecta,Noctuidae)

Summary In the noctuid moth Spodoptera exempta, the distribution of visual pigments within the fused rhabdoms of the compound eyes was investigated by electron microscopy. Each ommatidium regularly contains eight receptor cells belonging to three morphological types: one distal, six medial, and one basal cell (Meinecke 1981); four different visual pigments — absorption maxima at approximately 355, 465, 515, and 560 nm — are known to occur within the eye (Langer et al. 1979). The compound eyes were illuminated in situ by use of monochromatic light of different wavelengths. This illumination produced a wide scale of structural changes in the microvilli of the rhabdomeres of individual cells. Preparation of eyes by freeze-substitution revealed the structural changes in the rhabdomeres to be effects of light occurring in vivo.The degree of structural changes may be considerably different in rhabdomeres within the same ommatidium; it was found to depend on the wavelength and the duration of illumination, the intensity received by the ommatidia as well as the spectral sensitivity of the receptor cells. Therefore, it was possible to estimate the spectral sensitivities of the morphological types of receptor cells. Generally, all medial cells are green receptors and all basal cells red receptors; distal cells are blue receptors in about two-thirds of the ommatidia, while in the remaining third of them distal cells are sensitive to ultraviolet light.Supported by Deutsche Forschungsgemeinschaft, Sonderforschungsbereich 114 (Bionach)     

The rhodopsin system of the squid

Squid rhodopsin (λ_max 493 mµ)—like vertebrate rhodopsins—contains a retinene chromophore linked to a protein, opsin. Light transforms rhodopsin to lumi- and metarhodopsin. However, whereas vertebrate metarhodopsin at physiological temperatures decomposes into retinene and opsin, squid metarhodopsin is stable. Light also converts squid metarhodopsin to rhodopsin. Rhodopsin is therefore regenerated from metarhodopsin in the light. Irradiation of rhodopsin or metarhodopsin produces a steady state by promoting the reactions, See PDF for Equation Squid rhodopsin contains neo-b (11-cis) retinene; metarhodopsin all-trans retinene. The interconversion of rhodopsin and metarhodopsin involves only the stereoisomerization of their chromophores. Squid metarhodopsin is a pH indicator, red (λ_max 500 mµ) near neutrality, yellow (λ_max 380 mµ) in alkaline solution. The two forms—acid and alkaline metarhodopsin—are interconverted according to the equation, Alkaline metarhodopsin + H⁺ acid metarhodopsin, with pK 7.7. In both forms, retinene is attached to opsin at the same site as in rhodopsin. However, metarhodopsin decomposes more readily than rhodopsin into retinene and opsin. The opsins apparently fit the shape of the neo-b chromophore. When light isomerizes the chromophore to the all-trans configuration, squid opsin accepts the all-trans chromophore, while vertebrate opsins do not and hence release all-trans retinene. Light triggers vision by affecting directly the shape of the retinene chromophore. This changes its relationship with opsin, so initiating a train of chemical reactions.     

Renewal of visual pigment in photoreceptors of the blowfly

Summary Spectrophotometric measurements of photoreceptors 1–6 in the blowfly demonstrate that rhodopsin undergoes a continuous renewal. This involves, in the dark, the slow degradation of rhodopsin whereas metarhodopsin is degraded at a much faster rate. The effect of light is to reduce the rate at which metarhodopsin is degraded, i.e. the rate is inversely related to the intensity of the light. Rhodopsin synthesis is dependent on the presence of 11-cis retinal which is formed via a photoreaction from all-trans retinal resulting from the breakdown of rhodopsin and/or metarhodopsin: the biosynthesis of rhodopsin is therefore a light dependent process. Light of the blue/violet spectral range was found to mediate the isomerization of all-trans retinal into the 11-cis form. It is proposed that this stereospecificity is the result of all-trans retinal being bound to a protein. On the basis of the results a visual pigment cycle is proposed.     

The visual pigment and visual cycle of the lobster,Homarus

Summary The visual pigment of the American lobster,Homarus americanus, has been studied in individual isolated rhabdoms by microspectrophotometry. Lobster rhodopsin has _max at 515 nm and is converted by light to a stable metarhodopsin with _max at 490 nm. These figures are in good agreement with corresponding values obtained by Wald and Hubbard (1957) in digitonin extracts. Photoregeneration of rhodopsin to metarhodopsin is also observed. The absorbance spectrum of lobster metarhodopsin is invariant with pH in the range 5.4–9, indicating that even after isomerization of the chromophore fromcis totrans, the binding site of the chromophore remains sequestered from the solvent environment. Total axial density of the lobster rhabdom to unpolarized light is about 0.7.As described for several other Crustacea, aldehyde fixation renders the metarhodopsin susceptible to photobleaching, a process that is faster at alkaline than at neutral or acid pH. Small amounts of a photoproduct with _max at 370 nm are occasionally seen. A slower dark bleaching of lobster rhabdoms (_1/2–2 h) also occurs, frequently through intermediates with absorption similar to metarhodopsin.The molar extinction coefficient of metarhodopsin is about 1.2 times greater than that of rhodopsin, each measured at their respective _max. Isomerization of the chromophore fromcis totrans is accompanied by a change in the orientation of the absorption vector of about 3°. The absorption vector of metarhodopsin is either tilted more steeply into the membrane or is less tightly oriented with respect to the microvillar axes.When living lobsters are kept at room temperature, light adaptation does not result in an accumulation of metarhodopsin. At 4 °C, however, the same adapting lights cause a reduction of rhodopsin and an increase in metarhodopsin. There is thus a temperature-sensitive regeneration mechanism that supplements photoregeneration. Following 1 ms, 0.1 joule xenon flashes that convert about 70% of the rhodopsin to metarhodopsin in vivo, dark regeneration occurs in the living eye with half-times of about 25 and 55 min at 22 °C and 15 °C respectively.This work was supported by USPHS research grant EY 00222 to Yale University. S.N.B. was aided by NIH Postdoctoral Fellowship EY 52378.     

Visual pigment spectra of the comma butterfly,<Emphasis Type="Italic"> Polygonia c-album</Emphasis>, derived from in vivo epi-illumination microspectrophotometry

The visual pigments in the compound eye of the comma butterfly, Polygonia c-album, were investigated in a specially designed epi-illumination microspectrophotometer. Absorption changes due to photochemical conversions of the visual pigments, or due to light-independent visual pigment decay and regeneration, were studied by measuring the eye shine, i.e., the light reflected from the tapetum located in each ommatidium proximal to the visual pigment-bearing rhabdom. The obtained absorbance difference spectra demonstrated the dominant presence of a green visual pigment. The rhodopsin and its metarhodopsin have absorption peak wavelengths at 532 nm and 492 nm, respectively. The metarhodopsin is removed from the rhabdom with a time constant of 15 min and the rhodopsin is regenerated with a time constant of 59 min (room temperature). A UV rhodopsin with metarhodopsin absorbing maximally at 467 nm was revealed, and evidence for a blue rhodopsin was obtained indirectly.     

The dorsal eye of the dragonfly Sympetrum: specializations for prey detection against the blue sky

Dragonflies of the genus Sympetrum have compound eyes conspicuously divided into dorsal and ventral regions. Using anatomical, optical, electrophysiological, in-vivo photochemical and microspectrophotometrical methods, we have investigated the design and physiology of the dorsal part which is characterized by a pale yellow-orange screening pigment and extremely large facets. The upper part of the yellow dorsal region is a pronounced fovea with interommatidial angles approaching 0.3°, contrasting to the much larger values of 1.5°–2° in the rest of the eye. The dorsal eye part is exclusively sensitive to short wavelengths (below 520 nm). It contains predominantly blue-receptors with a sensitivity maximum at 420 nm, and a smaller amount of UV-receptors. The metarhodopsin of the blue-receptors absorbs maximally at 535 nm. The yellow screening pigment transmits longwavelength light (cut-on 580 nm), which increases the conversion rate from metarhodopsin to rhodopsin (see Fig. 11a). We demonstrate that because of the yellow pigment screen nearly all of the photopigment is in the rhodopsin state under natural conditions, thus maximizing sensitivity. Theoretical considerations show that the extremely long rhabdoms (1.1 mm) in the dorsal fovea are motivated for absorption reasons alone. A surprising consequence of the long rhabdoms is that the sensitivity gain, caused by pumping photopigment into the rhodopsin state, is small. To explain this puzzling fact we present arguments for a mechanism producing a gradient of rhodopsin concentration along the rhabdom, which would minimize saturation of transduction units, and hence improve the signal-to-noise ratio at high intensities. The latter is of special importance for the short integration time and high contrast sensitivity these animals need for spotting small prey at long distances.Abbreviations ERG electroretinogram - R rhodopsin - M metarhodopsin     

Distribution of rhodopsin and retinochrome in the squid retina

The cephalopod retina contains two kinds of photopigments, rhodopsin and retinochrome. For many years retinochrome has been thought to be localized in the inner segments of the visual cells, whereas rhodopsin is in the outer segments. However, it is now clear that retinochrome can be extracted also from fragments of outer segments. In the dark-adapted retina of Loligo pealei retinochrome is distributed half-and-half in the inner and outer segments. Todarodes pacificus contains much more retinochrome than Loligo, and it is more abundant in the outer than in the inner segments. The outer segments of Loligo contain retinochrome and metarhodopsin in addition to rhodopsin, whether squids are kept in the dark or in the light. But there is extremely little metarhodopsin (about 3% of rhodopsin) even in light-adapted eyes. The inner segments contain only retinochrome, and much less in the light than in the dark. On the other hand, retinochrome in the outer segments increases markedly during light adaptation. These facts suggest the possibility that some retinochrome moves forward from the inner to the outer segments during light adaptation and there reacts with metarhodopsin to promote regeneration of rhodopsin.     

Dark regeneration of rhodopsin in crayfish photoreceptors

The eyes of crayfish were exposed to lights of known spectral composition, and the course of regeneration was followed in the dark by measuring the content of rhodopsin and metarhodopsin in single rhabdoms isolated at various times after the adaptation, using an assay that is based on the fluorescence of metarhodopsin. Complete recovery requires several days in the dark after intense adaptation to orange light, but requires less than 2 d after blue light exposure. Following an orange light exposure with blue produces recovery kinetics characteristic of the blue light exposure alone. This quickening of recovery occurs whether the receptors are exposed to blue light either immediately or many hours after the original exposure to orange. Conversely, following blue light adaptation with orange leads to slow recovery, which is characteristic of orange alone. Recovery from long-wavelength adaptation is slower principally because many rhabdoms seem to delay the onset of regeneration. We suggest that the regeneration system is itself photosensitive, and after orange light adaptation the supply of active chromophore (presumably 11-cis retinal) limits the rate of recovery. Once started, recovery proceeds slowly and continuously, and the total pigment concentration (rhodopsin plus metarhodopsin) in the rhabdomeric membrane remains approximately constant. Within hours after intense adapting exposures, the rhabdoms become altered in appearance, the surfaces become coated with accessory pigment, and the bands of microvilli are less distinct. These changes persist until recovery of rhodopsin proceeds, which suggests that visual pigment regeneration results from addition of newly synthesized rhodopsin associated with membrane turn-over.     

Die Wirkung von Rotlicht und Blaulicht auf die Photosynthese von Acetabularia mediterranea

Zusammenfassung Die Photosynthese-Rate von Acetabularia mediterranea stellt sich in blauer Strahlung (350–500 nm) auf ein bestimmtes Niveau ein, in roter Strahlung (600–700 nm) fällt sie dagegen innerhalb von 2–3 Wochen bis ungefähr auf den Kompensationspunkt ab (Abb. 1). Der Photosyntheseapparat wird jedoch durch Rotlicht nicht irreversibel geschädigt, denn nach Bestrahlung mit Blaulicht steigt die Photosynthese-Rate in ca. 3 Tagen wieder auf den Ausgangswert an (Abb. 5). Dem Anstieg geht eine lag-Phase von mehreren Stunden voraus (Abb. 10). Photosynthese kann auch induziert werden, wenn die Bestrahlung mit Rotlicht kurzfristig täglich durch Blaulicht unterbrochen wird. Die erreichte Photosynthese-Rate hängt von der täglichen Blaulichtmenge ab und ist wahrscheinlich proportional dem Logarithmus der Blaulichtmenge.Die Wirkung roter und blauer Strahlung und zusätzlicher blauer Strahlung zum Rotlicht auf das Zellwachstum und die Substanzproduktion läßt sich zwanglos durch den Einfluß der Strahlung auf die Photosynthese-Rate der Zelle erklären.

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The influence of red light and blue light on the photosynthetic activity of Acetabularia mediterranea

Summary In blue light (350–500 nm) the rate of photosynthesis (oxygen evolution) of Acetabularia is almost constant after a short period of transition (Fig. 1). In red light (600–700 nm), however, it decreases within 2–3 weeks almost to zero (compensation point). The photosynthetic apparatus is not damaged irreversibly by red light, because transfering the cell from continuous red light (2 weeks) to continous blue light results in an increase of the rate of photosynthesis within 3 days up to the level in blue light (Fig. 5). Photosynthesis can also be stimulated if continuous red light is interrupted daily by short breaks of blue light. The rate of photosynthesis at the end of the induction period depends upon the amount of blue light per day (Fig. 5 and 6) and is probably proportional to the logarithm of this amount.Cell growth (Figs. 2, 7, 8) and formation of dry matter (Figs. 3, 9) in continuous red light, in blue light and in continuous red light supplemented by blue light is controlled by the rate of photosynthesis under these light condition.

     

Photopigment and receptor properties in Drosophila compound eye and ocellar receptors

A review of the spectral sensitivity and the rhodopsin and metarhodopsin characteristics in three compound eye receptor types (R1–6, R7, and R8) and ocellar receptors is presented (Fig. 1). Photopigment properties were determined from measures of conversion efficiency. The photopigments of R1–6 were studied using in vivo microspectrophotometry in the deep pseudopupil of white-eyed flies. These studies yielded a refined estimate of the R1–6 metarhodopsin spectrum (Fig. 2). The quantum efficiency relative to the spectral sensitivity estimate of the rhodopsin spectrum was factored out. The quantum efficiency of rhodopsin is about 1.75 times that of metarhodopsin. The peak absorbance of metarhodopsin was estimated to be about 2.6 times that of rhodopsin. The mechanism of the two-peaked R1–6 spectral sensitivity and metarhodopsin spectrum is discussed in terms of evidence that there is only one rhodopsin in R1–6 and that vitamin A deprivation preferentially lowers ultraviolet sensitivity. The prolonged depolarizing afterpotential is reviewed from the standpoint of the internal transmitter hypothesis of visual excitation. A careful comparison of the intensity-responsivity for photopigment conversion and its adaptional consequences is made (Fig. 3).     

Light inhibition of internode elongation in green plants

The clongation of the first internode of fully greenVigna sinensis L. is inhibited by white light (W). This inhibition is fluence-rate dependent between 0 and 70 Wm^–2. The kinetics of elongation rate in the light after darkness were investigated with linear displacement transducers. The internode elongation rate does not exhibit any endogenous rhythm. A rapid inhibition occurs during the first 2 or 3 h after the onset of light, and a second type of inhibition (slow reaction) increases from the beginning to the 8th hour of light. The rapid inhibition is not fluence-rate dependent between 20 and 70 Wm^–2, but the slow reaction is. There is no rapid inhibition in a low fluence rate white light to high fluence rate white light transition, only the slow reaction is observed. The responses to different wavebands, i.e., blue light (B), yellow and green light (YG), and red light (R), are the same for the two inhibition reactions. Each waveband used separately does not reproduce the full effect observed in W. Results show a stimulation with B, a greater inhibition activity with YG than with R, and a synergistic action of B and R which when given together lead to an inhibition similar to that obtained in W. Plants returned from the light to darkness progressively recover a high elongation rate without any latent period. The W light regulating internode elongation rate is mainly perceived by the growing internode itself.Abbreviations B blue light - D darkness - F far-red light - HW high fluence rate white light - LW low fluence rate white light - R red light - W white light - YG yellow and green light     

Light effects on in vitro rooting of pear cultivars of different rhizogenic ability

The effect of varying light regimes on in vitro rooting of microcuttings of two pear (Pyrus communis L.) cultivars was investigated. Cultures of the easy to-root Conference and the difficult-to-root Doyenne d'Hiver were incubated for 21 days with or without indole-3-butyric acid (IBA) in the medium in darkness or under continuous far-red (8 µmol m^–2 s^–1), blue, white or red (15 or 36 µmol m^–2 s^–1) light. Conference rooted without IBA when exposed to red, blue or white light while no rooting was observed under far-red light and in darkness. The high rooting efficiency under red and, by contrast, the inhibition under far-red light and darkness suggest the involvement of the phytochrome system in rhizogenesis. The addition of IBA to the culture medium enhanced root production under all light regimes in both cultivars. Red light, especially at the lower photon fluence rate, had a positive effect by increasing root extension (number × length of roots) and stimulating secondary root formation.Abbreviations IBA Indole-3-butyric acid - R red light - B blue light - FR far-red light - W white light - D darkness - P_fr active (far-red light absorbing) form of phytochrome - P_tot total phytochrome - BA benzyl-adenine     

Response of Audouinella saviana (Meneghini) Woelkerling (Nemaliales,Rhodophyta) cultures to monochromatic light

Audouinella saviana (Meneghini) Woelkerling was cultured at a constant temperature (24 °C) and different irradiances (from 1 µmol to 30 µmol photons m^–2 s^–1) of blue (430–470 nm) and green (500–560 nm) light in order to study its adaptive response. Modifications in colour, morphology and ultrastructure of the thalli, together with changes in pigment composition and in the spectral properties of chlorophyll a and R-phycoerythrin, were observed both by means of light and electron microscopy (TEM, SEM) and spectrophotometric and spectrofluorimetric analyses. In this paper we report the adaptive response of the seaweed to blue and green radiation by focussing on the cell wall and on the photosynthetic apparatus, particularly on phycobilisomes in situ and on R-PE after extraction. PBSs were fully structured only under blue light at low irradiance whilst they were absent under green light, whatever the irradiance, in spite of the high R-PE content. This fact, together with the spectral changes of R-PE, suggests adaptation at a molecular level, presumably referable to changes in aggregation state.