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PubMed2002

Light regulation of carotenoid biosynthesis in the prasinophycean alga Mantoniella squamata.

We have studied carotenoid biosynthesis in the prasinophycean alga Mantoniella squamata, which contains a great variety of carotenoids belonging to both the alpha- and the beta-carotene (Car) biosyntheses pathways. This unusual carotenoid composition allowed us to address the problem of how biosynthesis on the alpha- and the beta-Car pathway is regulated in response to different light regimes. We found that illumination with 4 h of actinic high light (HL, 250 micromol m(-2) s(-1)), and culture growth in permanent light (PL, 60 micromol m(-2) s(-1)). induced the de novo synthesis of violaxanthin (Vx) cycle pigments belonging to the beta-Car pathway. Carotenoid synthesis on the alpha-Car biosynthesis pathway led to a strong accumulation of lutein (L) and dihydrolutein (DhL). Both the newly synthesised Vx cycle pigments and L/DhL can be regarded as intermediate pools of carotenoids that were converted to light-harvesting pigments in low light (LL) periods following the phases of HL illumination. This transition to the light-harvesting pigments included the conversion of Vx to neoxanthin (Nx) on the beta-Car pathway, and the transformation of L/DhL to prasinoxanthin (Px), the main light-harvesting pigment of M. squamata belonging to the alpha-carotenoids. Isolation of light-harvesting complexes from L-enriched M. squamata cells showed that both L and the Vx cycle pigments were loosely bound to the LHC apoprotein. This peripheral binding is in agreement with their proposed role as intermediate pigments in the biosynthesis of light-harvesting pigments, and should allow a smooth detachment from the protein in periods of LL when the synthesis of Nx and Px is stimulated. We conclude that carotenoid synthesis proceeds in general in an economical way: in both, the alpha- and the beta-Car pathway HL induces the formation of photoprotective pigments, which in LL periods following the HL illumination are not degraded, but on the contrary are converted to light-harvesting pigments.

Carotenoids↗
PubMed2003

Water quality test based on dielectrophoretic measurements of fresh water algae Selenastrum capricornutum.

A method is described whereby dielectrophoresis of algal cells is used to perform rapid water quality analysis, specifically detecting the presence of CuSO4. The dielectric collection spectrum of the fresh water alga Selenastrum capricornutum was determined for a range of concentrations of CuSO4 from 25 mg L(-1) to 0.25 mg L(-1) for exposure times of 15 min and 18 h. In all cases increasing the concentration of CuSO4 reduced cell collection, but a step reduction was observed in collection between 2 mg L(-1) and 5 mg L(-1). This method has potential for forming a rapid, low-cost test for water quality with broad specificity and significantly reduced analysis time compared to current methods.

Chlorophyta↗
PubMed2005

Short- and long-term effects of solar ultraviolet radiation on the red algae Porphyridium cruentum (S. F. Gray) Nägeli.

During spring 2002 and fall 2003 we carried out experiment in tropical southern China to determine the short- and long-term effects of solar ultraviolet radiation (UVR, 280-400 nm) on photosynthesis and growth in the unicellular red alga Porphyridium cruentum. During the experimentation, cells of P. cruentum were exposed to three radiation treatments: (a) samples exposed to PAR (400-700 nm) + UV-A (315-400 nm) + UV-B (280-315 nm)(PAB treatment); (b) samples exposed to PAR + UV-A (PA treatment) and, (c) samples exposed only to PAR (P treatment). To assess the short-term impact of UVR as a function of irradiance, we determined photosynthesis versus irradiance (Pvs.E) curves. From these curves the maximum carbon uptake rate (P(max)) and the light saturation parameter (E(k)) were obtained, with values of approximately 12.8-14.4 microg C (microg chl a)(-1) h(-1), and approximately 250 micromol m(-2) s(-1), respectively. A significant UVR effect on assimilation numbers was observed when samples were exposed at irradiances higher than E(k), with samples exposed to full solar radiation having significant less carbon fixation than those exposed only to PAR. Biological weighting functions of P. cruentum were used to evaluate the UVR impact per unit energy received by the cells; the data indicate that the species is as sensitive as natural phytoplankton from the southern China Sea; however, it is much more resistant than Antarctic assemblages. When evaluating the combined effects of mixing speed and UVR, it was seen that samples rotating fast within the upper mixed layer were less inhibited by UVR as compared to those under slow mixing or in fixed samples. Growth of P. cruentum over a week-long experiment was not affected by neither UVR nor UV-A; additionally, low photoinhibition was found at the end as compared to that at the beginning of this experiment. Our results thus indicate that, although on short-term basis P. cruentum is affected by solar UVR, it can acclimate to minimize UVR-induced effects when given enough time.

Dose-Response Relationship, Radiation↗
PubMed2005

First report on the detection and quantification of arsenobetaine in extracts of marine algae using HPLC-ES-MS/MS.

The detection of arsenobetaine in extracts of marine algae is reported here for the first time. The application of liquid chromatography coupled online with electrospray tandem mass spectrometry in the selected reaction monitoring mode provided improved performance for the detection of low amounts of arsenobetaine in the presence of high amounts of arsenosugars.

Arsenicals↗
PubMed1966

Isolation and identification of carotenoids produced by a green alga (Dictyococcus cinnabarinus) in submerged culture.

1. Six carotenoid pigments were produced by and isolated from the green alga Dictyococcus cinnabarinus grown in submerged culture in the presence of glucose. 2. The first, second and fourth pigments were identified respectively as beta-carotene, echinenone and canthaxanthin; the physicochemical properties of the other three are described and their similarity to other oxo-carotenoids is shown. 3. Culture techniques, isolation and identification procedures are described.

Journal Article↗
PubMed1968

C-phycocyanin and allophycocyanin in two species of blue-green algae.

1. The biliproteins C-phycocyanin and allophycocyanin were purified from the blue-green alga Anabaena variabilis by ammonium sulphate fractionation and gel filtration. 2. An assay procedure that enabled the proportion of the two pigments, present as a mixture, to be determined was devised by using the data provided by spectrophotometric analysis of the purified biliproteins. 3. The degree of association and relative proportions of the two pigments were analysed by the application of this procedure to the components separated by thin-layer gel filtration. 4. The C-phycocyanin/allophycocyanin ratio remained essentially constant in algal extracts prepared at various stages throughout the growth cycle or after growth under conditions of reduced illumination. 5. The behaviour of the C-phycocyanin aggregate species from Anacystis nidulans suggested that they were of appreciably lower molecular weight than those observed in extracts of Anabaena variabilis.

Cell-Free System↗
PubMed1975

The amino acid sequence of cytochrome f from the brown alga Alaria esculenta (L.) Grev.

Cytochrome f was isolated from the brown alga Alaria esculenta and the amino acid sequence was determined. The native haemoprotein has a molecular weight of 9800 and consists of a single polypeptide chain of 86 amino acid residues with a haem group bonded to cysteine residues at positions 14 and 17. The N-terminus is not acetylated and no methylated lysines were found. Sequences of three other algal cytochromes f were compared with that of Alaria and 22 out of 92 positions were common to the four sequences. One-half of these conserved sites occur between positions 49 and 63. Detailed evidence for the amino acid sequence of Alaria cytochrome has been deposited as Supplementary Publication SUP 50048 (6 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975) 145, 5.

Amino Acid Sequence↗
PubMed1976

Phospholipid composition of the plasma membrane of the green alga, Hydrodictyon africanum.

A plasma-membrane fraction was isolated from the alga Hydrodictyon africanum by micro-dissection and its phospholipid components were analysed. Phosphatidylcholine was the major phospholipid of the preparation. Both phosphatidylserine and diphosphatidylglycerol were enriched in the fraction compared with the whole cell, but the relative amount of phosphatidylglycerol present was less than that in the whole cell. Phosphatidylinositol was absent from the plasma-membrane preparation.

Cell Membrane↗
PubMed1977

The covalent linkage of protein to carbohydrate in the extracellular protein-polysaccharide from the red alga Porphyridium cruentum.

The extracellular anionic polysaccharide isolated from cultures of a unicellular red alga, Porphyridium cruentum, contains a small amount of protein after extensive purification. The polysaccharide and protein are recovered in the same fraction after isopycnic CsCl-density-gradient centrifugation in 4M-guanidinium chloride, under conditions designed to separate proteins from polysaccharide. The peptide portion of the protein-polysaccharide is released from the polysaccharide by alkali under conditions for beta-elimination. The released peptide is non-diffusible, but in can be separated from the polysaccharide by precipitation of the polysaccharide as the cetylpyridinium complex. Under conditions for beta-elimination of certain O-glycosidic carbohydrate-protein linkages, selective destruction of serine and threonine occurs. The addition of a reducing agent to the alkali mixture produces a selective increase in alanine and alpha-aminobutyric acid. Addition of a tritiated reducing agent to the alkali mixture produces radioactive alanine and alpha-aminobutyric acid, and xylitol as the only sugar alcohol. Similar results are obtained from glycopeptides isolated from partial acid hydrolysates. A macromolecular structure of the protein-polysaccharide is suggested by a comparison of the intrinsic viscosity of material before and after treatment with alkali and proteolytic enzymes.

Amino Acids↗
PubMed1979

Mössbauer spectra of photosystem-I-reaction centres from the blue-green alga Chlorogloea fritschii.

Substantial amounts of iron have been shown by Mössbauer spectroscopy to be present in Photosystem-I preparations from the blue-green alga Chlorogloeta fritschii. Changes in the spectra on chemical reduction provide evidence that some of this iron is very similar to that found in the 4Fe-4S centres of ferredoxins. Such reduced samples also show e.p.r. signals consistent with maximum reduction of iron-sulphur centres A and B of Photosystem I. An unchanged component in the spectra indicates, assuming all centres A and B are reduced, the presence of another iron-containing species.

Cell Membrane↗
PubMed1981

Properties of oxygen-evolving photosystem-II particles from Phormidium laminosum, a thermophilic blue--green alga.

1. O2-evolving Photosystem-II particles from the thermophilic blue--green alga Phormidium laminosum contained 1 mol of Mn/13--17 mol of chlorophyll a compared with 1 mol of Mn/65--75 mol of chlorophyll a in unfractionated membranes. 2. At least two-thirds of the Mn in the Photosystem-II particles was removed by mild heating and by treatment with Tris or EDTA, with concomitant loss of O2 evolution. However, irreversible inactivation was also caused by washing in buffers without MgCl2, and this inactivation was not accompanied by a corresponding loss of Mn. 3. Bivalent cations (Mg2+ or Ca2+), Cl- or Br- ions and at least 20% (v/v) glycerol were required for maximum stability of O2 evolution. 4. The Photosystem-II particles were enriched in high-potential cytochrome b-559 (1 mol of cytochrome/50--60 mol of chlorophyll a) and in component C-550, and had a photosynthetic-unit size of 40--70 molecules of chlorophyll a. 5. The absorption spectrum at 77 K showed a preponderance of shorter-wavelength forms of chlorophyll a in the Photosystem-II particles, and in the fluorescence emission spectrum at 77 K there were major chlorophyll fluorescence bands at 684 nm and 695 nm, with almost no fluorescence in the far-red region. 6. Analysis of the lipid and protein contents showed that the Photosystem-II particles were not chemically pure (for example, all of the membrane-bound cytochromes and cytochrome c-549 were present), but their high O2-evolution activity and good optical properties make them useful for functional studies on Photosystem-II and O2 evolution.

Chloroplasts↗
PubMed1984

Ferrochelatase activity in the photosynthetic alga Cyanidium caldarium. Development of the enzyme during biosynthesis of photosynthetic pigments.

Dark-grown cells of the photosynthetic alga Cyanidium caldarium were shown to contain ferrochelatase activity, which increased markedly when the cells were induced to form pigments by exposure to light. Km values for the crude enzyme preparation were 14.8 microM and 6.5 microM for binding of Co2+ and deuteroporphyrin IX respectively.

Ferrochelatase↗
PubMed1987

Characterization of a low-relative-molecular-mass prolyl 4-hydroxylase from the green alga Chlamydomonas reinhardii.

Prolyl 4-hydroxylase was partially purified and characterized from the unicellular green alga, Chlamydomonas reinhardii. This enzyme differed from all the animal and plant prolyl 4-hydroxylases studied so far in that its Mr was only about 40,000 by gel filtration, being thus less than one-sixth of those determined for the vertebrate and higher-plant enzymes. The algal enzyme did not hydroxylate to any significant extent chick-embryo protocollagen or triple-helical (Pro-Pro-Gly)10, whereas a low hydroxylation rate was found with denatured (Pro-Pro-Gly)10. Poly(L-proline), which is an effective inhibitor of the vertebrate enzymes but acts as a substrate for some higher-plant enzymes, was a good substrate. In the absence of poly(L-proline) the enzyme catalysed an uncoupled decarboxylation of 2-oxoglutarate. Studies of the Km values for the co-substrates and cofactors and the specificity of the 2-oxoglutarate requirement, as well as inhibition studies with selected 2-oxoglutarate analogues, suggested that the catalytic site of the algal enzyme is similar to, but not identical with, those of the vertebrate enzymes. The existence of distinct similarities was further demonstrated by an inhibition of the algal enzyme activity with a monoclonal antibody to the beta-subunit of human prolyl 4-hydroxylase. The amount of prolyl 4-hydroxylase activity in the algal cells was not altered by signals which recognize the presence or absence of the cell wall, as determined in studies on experimental cell-wall regeneration and wall-less mutants.

Cell Wall↗
PubMed1989

The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus.

The amino acid sequence of the constitutive flavodoxin from the red alga Chondrus crispus was determined from the analyses of peptide fragments derived by enzymic digestions of the carboxymethylated protein. This is the first sequence reported for a flavodoxin from a eukaryote. The protein is composed of 173 amino acid residues and is a member of the longer-chain group of flavodoxins. The extent of sequence homology to the three other flavodoxins in the group for which sequences are available is in the range 36-39%, with the most strongly conserved regions being those implicated in binding of the FMN, the redox-active prosthetic group. Nevertheless, Chondrus crispus flavodoxin stands apart in a number of respects, in particular the possession of an unusually high content of proline, with these residues distributed more or less regularly along the peptide chain.

Amino Acid Sequence↗
PubMed1990

Purification and characterization of protein disulphide-isomerase from the unicellular green alga Chlamydomonas reinhardii. A 120 kDa dimer antigenically distinct from the vertebrate enzyme.

Protein disulphide-isomerase (PDI) has been isolated from the unicellular green alga Chlamydomonas reinhardii and purified by (NH4)2SO4 precipitation, gel filtration and DEAE-Sephacel, hydroxyapatite and f.p.l.c. chromatography. The active algal enzyme is a 120 kDa dimer with a subunit molecular mass of 60 kDa when determined by SDS/PAGE. Although similar in size to the previously isolated vertebrate PDIs, the algal enzyme is antigenically distinct, polyclonal antibodies against the algal PDI showing no cross-reactivity with the vertebrate enzyme on immunoblots, and vice versa. The anti-(algal PDI) antiserum did not inhibit algal PDI activity, and C. reinhardii PDI could be immobilized on anti-PDI-Protein A-Sepharose in active form. In contrast with the situation in vertebrates, where PDI functions as a subunit of prolyl 4-hydroxylase, the C. reinhardii PDI is not associated with the algal prolyl 4-hydroxylase.

Chlamydomonas↗
PubMed1994

The green alga Scenedesmus obliquus contains both diadenosine 5',5'''-P1,P4-tetraphosphate (asymmetrical) pyrophosphohydrolase and phosphorylase activities.

Diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) phosphorylase and Ap4A pyrophosphohydrolase activities have been purified from extracts of the green alga Scenedesmus obliquus. Both activities were also detected in Scenedesmus brasiliensis, Scenedesmus quadricauda and in Chlorella vulgaris. This is the first time that both types of enzyme have been detected in the same species. The Ap4A phosphorylase has a molecular mass of 46-48 kDa, a broad pH optimum between 7.5 and 9.5, and requires a divalent ion for activity (Mg2+ > Co2+ > Ca2+ = Mn2+ = Cd2+ > Zn2+). It degrades substrates with at least four phosphate groups and always produces a nucleoside 5'-diphosphate product. The Km values for Ap4A and Pi are 5.3 microM and 160 microM, respectively, and kcat. = 1.8 s-1. Arsenate, vanadate, molybdate, chromate and tungstate can substitute for phosphate. The enzyme also catalyses Ap4A synthesis (Keq. = [Ap4A] [Pi]/[ATP][ADP] = 9 x 10(-4)) and ADP arsenolysis. The Ap4A hydrolase has a molecular mass of 26-28 kDa, an alkaline pH optimum of 8.8-9.8, and prefers Zn2+ as the stimulatory ion (Zn2+ > Mg2+ > Mn2+ > Co2+ > Cd2+). It degrades substrates with at least four phosphate groups, having a slight preference for Ap5A, and always produces a nucleoside 5'-triphosphate product. The Km value for Ap4A is 6.6 microM and kcat. = 1.3 s-1. It is inhibited competitively by adenosine 5'-tetraphosphate (Ki = 0.67 microM) and non-competitively by fluoride (Ki = 150 microM). A 50-54 kDa dinucleoside 5',5'''-P1,P3-triphosphate (Ap3A) pyrophosphohydrolase was also detected in S. obliquus, S. quadricauda and C. vulgaris. The corresponding enzyme in S. brasiliensis (> 100 kDa) may be a dimer

Acid Anhydride Hydrolases↗
PubMed1996

Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/glyceraldehyde 3-phosphate non-mevalonate pathway in the green alga Scenedesmus obliquus.

Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13C-NMR spectroscopy. According to the 13C-labelling pattern indicated by the 13C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids beta-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diphosphate), but via the novel glyceraldehyde 3-phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diphosphate involves the condensation of a C2 unit derived from pyruvate decarboxylation with glyceraldehyde 3-phosphate and a transposition yielding the branched C5 skeleton of isoprenic units.

Carbon Isotopes↗

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