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PubMed1991

Repetitive sequence-mediated rearrangements in Chlorella ellipsoidea chloroplast DNA: completion of nucleotide sequence of the large inverted repeat.

A 3454 base pair (bp) sequence of the large inverted repeat (IR) of chloroplast DNA (cpDNA) from the unicellular green alga Chlorella ellipsoidea has been determined. The sequence includes: (1) the boundaries between the IR and the large single copy (LSC) and the small single copy (SSC) regions, (2) the gene for psbA and (3) an approximately 1.0 kbp region between psbA and the rRNA genes which contains a variety of short dispersed repeats. The total size of the Chlorella IR was determined to be 15243 bp. The junction between the IR and the small single copy region is located close to the putative promoter of the rRNA operon (906 bp upstream of the -35 sequence on each IR). The junction between the IR and the large single copy region is also just upstream of the putative psbA promoter, 218 bp upstream from the ATG initiation codon. A few sets of unique sequences were found repeatedly around both junctions. Some of the sequences flanking the IR-LSC junction suggest a unidirectional and serial expansion of the IR within the genome. The psbA gene is located close to the LSC-side junction and codes for a protein of 352 amino acid residues. A highly conserved C-terminal Gly is absent Unlike the psbA of Chlamydomonas species, which contains 2-4 large introns, the gene of Chlorella has no introns.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1978

Physiological and biochemical contributions to the taxonomy of the genus Chlorella. XI. DNA hybridization.

1. DNA homology was studied in 12 Chlorella species. The DNA of 88 strains was hybridized with 3H-labelled DNA from C. fusca var. vacuolata 211-8 b and from C. vulgaris 211-8m. The results indicate that the genus Chlorella is a heterogenous taxon which consists of several groups of species. 2. The "C. fusca group" comprises C. fusca var. vacuolata, C. fusca var. rubescens, and C. zofingiensis. Within this group, C. zofingiensis appears to be more closely related to C. fusca var. vacuolata than is C. fusca var. rubescens. C. fusca var. fusca does not belong to this group of taxa. 3. The "C. vulgaris group" consists of C. vulgaris, C. sorokiniana, and C. saccharophila. There are several strains which seem to assume a position intermediate between C. vulgaris and C. saccharophila. C. protothecoides is not related to this group of species. 4. Several groups of strains of C. sorokiniana with different base compositions (guanine + cytosine content) of their DNA appear to belong to the same taxon. 5. In addition to C. fusca var. fusca and C. protothecoides, also C. luteoviridis, C. minutissima, C. kessleri, and C. homosphaera seem to have so little relationship with the other species that their assignment to the genus Chlorella appears questionable.

Chlorella↗
PubMed1976

[The metabolic interactions between Paramecium bursaria Ehrbg. and Chlorella spec. in the Paramecium bursaria-symbiosis. I. The nitrogen and the carbon metabolism (author's transl)].

Symbiotic Chlorellae have been isolated from Paramecium bursaria Ehrbg. and cultivated under conditions of nitrogen deficiency. Reinfection of Chlorella-free Paramecium bursaria with these nitrogen-deficient algae resulted in a complete regeneration and multiplication of the algae within the host cells. The endosymbiotic algal cells of the Paramecium bursaria-symbiosis can be supplied by their host with nitrogen. The inhibition of photosynthesis by 3-(3,4-Dichlorophenyl)-1,1-dimethylurea (DCMU) leads in green Paramecium bursaria to a breakdown of the symbiotic steady state-system resulting in a loss of algal cells. Obviously the endosymbiotic algae cannot be fed heterotrophically by their host to such an extent that a stable symbiosis is maintained. The application of 3-(3,4-Dichlorophenyl)-1,1-dimethylurea (DCMU) can be used as a new method for culturing Chlorella-free Paramecium bursaria.

Chlorella↗
PubMed1975

The regreening of nitrogen-deficient Chlorella fusca II. Structural changes during synchronous regreening.

Chlorella fusca, strain 211-15, cells degreened in a nitrogen-deficient mineral growth medium in the light for 4-6 weeks were regreened for up to 24 hrs in a nitrogen rich medium that leads to synchronous cell division at 24-26 hrs. Structural changes in the plastid membranes during the regreening period were observed by thin section and freeze-fracture electron microscopy. Nitrogen-deficient plastids were found to have non-appressed lamellae, prolamellar body-like membrane aggregations, and only 2 types of freeze-fracture face. At this time no photosynthetic oxygen evolution could be demonstrated. After 6 hrs regreening the plastid lamellae had fused to form bands of appressed lamellae and the four types of freeze-fracture face, described previously, were visible. At this time photosynthetic oxygen evolution could be demonstrated. After 24 hrs regreening the plastids had an appearance typical of normally grown Chlorella and had commenced to divide. Supporting evidence for these developmental stages is presented from isolated chloroplast particle fractions. An unusual type of cell wall proliferation was observed in the nitrogen-deficient Chlorella cells that resulted in the laying down of several walls, each with a trilaminar component.

Cell Division↗
PubMed1990

Phylogenetic position of some Chlorella species within the chlorococcales based upon complete small-subunit ribosomal RNA sequences.

Complete small-subunit rRNA (16S-like rRNA) coding region sequences were determined for eight species of the Chlorococcales (Chlorophyceae). The genera investigated include Prototheca, Ankistrodesmus, Scenedesmus, and five Chlorella species. Distance matrix methods were used to infer a phylogenetic tree that describes evolutionary relationships between several plant and green algal groups. The tree exhibits a bifurcation within the Chlorococcales consistent with the division into Oocystaceae and Scenedesmaceae, but three of the five Chlorella species are more similar to other algae than to Chlorella vulgaris. All of the sequences contain primary and secondary structural features that are characteristic of 16S-like rRNAs of chlorophytes and higher plants. Anikstrodesmus stipitatus, however, contains a 394-bp group I intervening sequence in its 16S-like rRNA coding region.

Base Sequence↗
PubMed2006

The effect of pH on the uptake and toxicity of copper and zinc in a tropical freshwater alga (Chlorella sp.).

Copper and zinc toxicity to the freshwater alga Chlorella sp. was determined at a range of pH values (5.5-8.0) in a synthetic softwater (hardness 40-48 mg CaCO(3)/L). The effects of the metals on algal growth (cell division) rate were determined after 48-h exposure at pH 5.5, 6.0, 6.5, 7.0, 7.5, and 8.0. The toxicity of both metals was pH dependent. As pH decreased from 8.0 to 5.5, the copper concentration required to inhibit the algal growth rate by 50% (IC50) increased from 1.0 to 19 microg/L. For zinc, the IC50 increased from 52 to 2,700 microg/L over the same pH range. Changes in solution speciation alone did not explain the increased toxicity observed as the pH increased. Modelled Cu(2+) and Zn(2+) concentrations decreased with increasing pH, whereas toxicity was observed to increase. Measurements of extracellular (cell-bound) metal concentrations support the biotic ligand model (BLM) theory of competition between protons (H(+)) and metals for binding sites at the algal cell surface. Higher extracellular metal concentrations were observed at high pH, indicating reduced competition. Independent of pH, both extracellular and intracellular copper were directly related to growth inhibition in Chlorella sp., whereas zinc toxicity was related to cell-bound zinc only. These findings suggest that the algal cell surface may be considered as the biotic ligand in further development of a chronic BLM with microalgae. Conditional binding constants (log K) were determined experimentally (using measured intracellular metal concentrations) and theoretically (using concentration-response curves) for copper and zinc for Chlorella sp. at selected pH values. Excellent agreement was found indicating the possibility of using concentration-response data to estimate conditional metal-cell binding constants.

Chlorella↗
PubMed1998

Purification, characterization and cDNA cloning of soluble carbonic anhydrase from Chlorella sorokiniana grown under ordinary air.

Soluble carbonic anhydrase (CA, EC 4.2.1.1) inducible by low levels of CO2 was purified from the unicellular green alga Chlorella sorokiniana grown at alkaline pH. The purified CA had a specific activity of 2,300 units (mg protein)-1. The molecular mass of the CA was found to be 100 kDa by non-dissociating (native)-polyacrylamide gel electrophoresis and 50 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The 50-kDa subunit was recognized by concanavalin A. These results suggest that the protein has a dimeric form with two 50-kDa subunits that are glycosylated in an asparagine-linked manner. The native CA was revealed by isoelectric focusing to be a very acidic protein with an isoelectric point of 4.2. About 60% of the CA activity was inhibited by 0.5 M NaCl. The enzyme was inactivated over 95% by preincubation with 50 mM dithiothreitol but not with 1 mM dithiothreitol. After partial amino acid sequence analysis, a cDNA clone of the CA was isolated and characterized. The cloned cDNA fragment encoded a 348-amino-acid polypeptide (36,709 Da) including an NH2-terminal hydrophobic signal peptide composed of 35 amino acids (3,725 Da). Conserved regions of sequences found in animal CAs, in the periplasmic (pCA) and the intracellular CAs of Chlamydomonas, and in the plasma-membrane-bound CA of Dunaliella (Dca) were also found in this Chlorella CA. The signal sequence was significantly homologous to the pCA and the Dca. The internal signal sequence between the large and the small subunits reported for pCA was not found in this Chlorella CA. The soluble CA of this alga was an alpha-type CA with salt-sensitive, periplasm-locating and acidic properties and very different from pCA and Dca with their salt-sensitive/neutral and salt-resistant/acidic properties, respectively.

Air↗
PubMed1999

Photoadaptation of two members of the Chlorophyta (Scenedesmus and Chlorella) in laboratory and outdoor cultures: changes in chlorophyll fluorescence quenching and the xanthophyll cycle.

The role of the xanthophyll cycle in the adaptation of two chlorococcal algae Scenedesmus quadricauda and Chlorella sorokiniana to high irradiance was studied under laboratory and outdoor conditions. We wished to elucidate whether the xanthophyll cycle plays a key role in dissipating the excesses of absorbed light, as in higher plants, and to characterise the relationship between chlorophyll fluorescence parameters and the content of xanthophyll-cycle pigments. The xanthophyll cycle was found to be operative in both species; however, its contribution to overall non-photochemical quenching (NPQ) could only be distinguished in Scenedesmus (15-20% of total NPQ). The Scenedesmus cultures showed a larger pool of xanthophyll-cycle pigments than Chlorella, and lower sensitivity to photoinhibition as judged from the reduction of maximum quantum yield of photosystem II. In general, both algae had a larger xanthophyll-cycle pool when grown outdoors than in laboratory cultures. Comparing the two species, Scenedesmus exhibited a higher capacity to adapt to high irradiance, due to an effective quenching mechanism and high photosynthetic capacity; in contrast, Chlorella represents a species with a larger antennae system, less-efficient quenching and lower photosynthetic performance. Non-photochemical quenching (NPQ) induced through the xanthophyll cycle can, to a limited extent, represent a regulatory factor in diluted algal cultures grown in outdoor solar photobioreactors, as well as in natural algal phytoplankton populations exposed transiently to high irradiance. However, it does not play an appreciable role in dense, well-mixed microalgal suspensions.

Adaptation, Physiological↗
PubMed1998

Structure of the Chlorella Zepp retrotransposon: nested Zepp clusters in the genome.

Zepp elements found in the telomeric region of Chlorella chromosomes show the characteristic features of non-viral (LINE-like) retrotransposons, including a poly(A) tail, 5' truncations, a retroviral reverse transcriptase-like ORF and flanking target duplications. We have isolated and characterized a full-length Zepp element (8943 bp long) from Chlorella chromosome V. Some peculiar features of this element, including nested integration, two ORF structures, a long 3' noncoding region and a possible promoter region are compared with those of the Drosophila telomeric retrotransposons HeT-A and TART. The Chlorella chromosome-Zepp system appears to represent an intermediate stage between canonical telomerase-telomeres and Drosophila retrotransposon-telomeres.

Amino Acid Sequence↗
PubMed2005

Symbiotic Chlorella sp. of the ciliate Paramecium bursaria do not prevent acidification and lysosomal fusion of host digestive vacuoles during infection.

Each symbiotic Chlorella sp. of the ciliate Paramecium bursaria is enclosed in a perialgal vacuole derived from the host digestive vacuole, and thereby the alga is protected from digestion by lysosomal fusion. Algae-free cells can be reinfected with algae isolated from algae-bearing cells by ingestion into digestive vacuoles. To examine the timing of acidification and lysosomal fusion of the digestive vacuoles and of algal escape from the digestive vacuole, algae-free cells were mixed with isolated algae or yeast cells stained with pH indicator dyes at 25+/-1 degrees C for 1.5 min, washed, chased, and fixed at various time points. Acidification of the vacuoles and digestion of Chlorella sp. began at 0.5 and 2 min after mixing, respectively. All single green Chlorella sp. that had been present in the host cytoplasm before 0.5 h after mixing were digested by 0.5 h. At 1 h after mixing, however, single green algae reappeared in the host cytoplasm, arising from those digestive vacuoles containing both nondigested and partially digested algae, and the percentage of such cells increased to about 40% at 3 h. At 48 h, the single green algae began to multiply by cell division, indicating that these algae had succeeded in establishing endosymbiosis. In contrast to previously published studies, our data show that an alga can successfully escape from the host's digestive vacuole after acidosomal and lysosomal fusion with the vacuole has occurred, in order to produce endosymbiosis.

Animals↗
PubMed2002

Purification of lipoxygenase from Chlorella: production of 9- and 13-hydroperoxide derivatives of linoleic acid.

Oxygenation of linoleic acid by the enzyme lipoxygenase (LOX) that is present in the microalga Chlorella pyrenoidosa is known to produce the corresponding 9- and 13-hydroperoxide derivatives of linoleic acid (9- and 13-HPOD, respectively). Previous work with this microalga indicated that partially purified LOX, present in the 30-45 and 45-80% saturated (NH4)2SO4 precipitate fractions, produced both HPOD isomers but in different ratios. It was not clear, however, if the observed activity in the two isolates represented the presence of one or more isozymes. In the present work, LOX isolated from the intracellular fraction of Chlorella by (NH4)2SO4 precipitation (35-80% saturated) was purified by ion exchange and hydrophobic interaction chromatography to apparent homogeneity. Analysis of the purified protein by SDS-PAGE and subsequent native size exclusion chromatography demonstrated that LOX in Chlorella is a single monomeric protein with a molecular mass of approximately 47 kDa. The purified LOX produced both the 9-HPOD and 13-HPOD isomers from linoleic acid in equal amounts, and the isomer ratio was not altered over the pH range of 6 to 9. Optimal activity of LOX was at pH 7.5.

Chlorella↗
PubMed1977

Kinetics of chlorophyll fluorescence at 77K in Chlorella and chloroplasts. Effects of CCCP, ferricyanide and DCMU.

The kinetics of chlorophyll fluorescence at 77K were studied in Chlorella cells and spinach chloroplasts. During a first illumination, the rise is polyphasic with at least three phases. The slowest one is irreversible and corresponds to the cytochrome oxidation. The dark regeneration of half the variable fluorescence is biphasic, the fast phase being inhibited by 3-(3,4-dichlorophenyl)-1, 1-dimethylurea (DCMU) both in Chlorella and chloroplasts. The fluorescence rise during a second illumination is still biphasic. Carbonyl cyanide m-chlorophenylhydrazone (CCCP) slows down the fluorescence rise in Chlorella but has no effect on the dark regeneration. It does not affect the fluorescence of chloroplasts. Ferricyanide which oxidizes cytochrome beta-559 at room temperature produces a quenching of the variable fluorescence and an acceleration of the fluorescence rise during the first illumination. Our results fit the idea of the heterogeneity of the Photosystem II centers at low temperature.

Carbonyl Cyanide m-Chlorophenyl Hydrazone↗
PubMed1977

Cyanide formation from histidine in Chlorella. A general reaction of aromatic amino acids catalyzed by amino acid oxidase systems.

The formation of HCN from D-histidine in Chlorella vulgaris extracts is shown to be due to the combined action of a soluble protein and a particulate component. Either horse-radish peroxidase (EC 1.11.1.7) or a metal ion with redox properties can be substituted for the particulate component. Ions of manganese and vanadium are especially effective, as are o-phenanthroline complexes of iron. Cobalt ions are less active. The D-amino acid oxidase (EC 1.4.3.3) from kidney and the L-amino acid oxidase (EC 1.4.3.2) from snake venom likewise cause HCN production from histidine when supplemented with the particulate preparation from Chlorella or with peroxidase or with a redox metal ion. The stereospecificity of the amino acid oxidase determines which of the two stereoisomers of histidine is active as an HCN precursor. Though histidine is the best substrate for HCN production, other naturally occurring aromatic amino acids (viz. tyrosine, phenylalanine and tryptophan) can also serve as HCN precursors with these enzyme systems. The relative effectiveness of each substrate varies with the amino acid oxidase enzyme and with the supplement. With respect to this latter property, the particulate preparation from Chlorella behaves more like a metal ion than like peroxidase.

Amino Acid Oxidoreductases↗
PubMed1977

A D-amino acid oxidase from Chlorella vulgaris.

A procedure has been developed for the partial purification from Chlorella vulgaris of an enzyme which catalyzes the formation of HCN from D-histidine when supplemented with peroxidase of a metal with redox properties. Some properties of the enzyme are described. Evidence is presented that the catalytic activity for HCN formation is associated with a capacity for catalyzing the oxidation of a wide variety of D-amino acids. With D-leucine, the best substrate for O2 consumption, 1 mol of ammonia is formed for half a mol of O2 consumed in the presence of catalase. An inactive apoenzyme can be obtained by acid ammonium sulfate precipitation, and reactivated by added FAD. On the basis of these criteria, the Chlorella enzyme can be classified as a D-amino acid oxidase (EC 1.4.3.3). Kidney D-amino acid oxidase and snake venom L-amino acid oxidase, which likewise form HCN from histidine on supplementation with peroxidase, have been compared with the Chlorella D-amino acid oxidase. The capacity of these enzymes for causing HCN formation from histidine is about proportional to their ability to catalyze the oxidation of histidine.

Animals↗
PubMed1988

A comparison of viruses infecting two different Chlorella-like green algae.

Five plaque-forming viruses (Pbi viruses) of the unicellular, eukaryotic, exsymbiotic Chlorella-like green alga strain Pbi were isolated from fresh water collected in Germany. The viruses were compared to two previously characterized plaque-forming viruses (NC64A viruses) of Chlorella strain NC64A. The Pbi viruses do not infect Chlorella NC64A and vice versa. Like the NC64A viruses the Pbi viruses are large polyhedron with a diameter of 140 to 150 nm, are chloroform sensitive, have many structural proteins, and have large dsDNA genomes of at least 300 kb. However, the Pbi viruses are serologically distinct from the NC64A viruses. The five Pbi virus genomes contain 5-methylcytosine, which varied from 14.2 to 43.1% of the cytosine, and two of them also contained N6-methyladenine. DNAs from the Pbi viruses hybridized poorly with the two NC64A virus DNAs and they have a higher guanine plus cytosine content (ca. 46%) than the NC64A virus DNAs (ca. 40%).

Base Composition↗
PubMed1989

Ultrastructural and growth indices of Chlorella culture in multicomponent aquatic systems under space flight conditions.

Submicroscopic organization of Chlorella cells cultivated under space flight conditions in three-component aquatic system has been studied. Comparison of the experimental cells with that of the controls revealed certain rearrangements of cell organelles particularly, a reduction in the amount of reserve polysaccharides in chloroplasts, increase of cell vacuolization and mitochondrion volume, complication configuration of plasmalemma evaginations and invaginations, and also disturbances in the process of cytokinesis. More over an increase in the number of Chlorella cells infected by bacteria was shown in the experimental variant. No considerable differences were established in the growth characteristics of the experimental and control populations. A comparative cytological analysis revealed general regularities of organelles in Chlorella cells cultivated under space flight condition in the uni- and multicomponent systems.

Aquaculture↗
PubMed1992

Peculiarities of the submicroscopic organization of Chlorella cells cultivated on a solid medium in microgravity.

The submicroscopic organization of Chlorella vulgaris cells (strain LARG-1) growing over 30 days on a solid agarized medium aboard the orbital station "Mir" was studied. A number of differences in the ultrastructure of cells of the experimental population compared to the control has been revealed. Thus, changes in the membrane system of plastids, in particular, appearance of numerous vesicles of different diameter and outgrowths of the plastids and their contact with the plasmalemma as well as a considerable decrease of reserve polysaccharide number in the plastids. Moreover, an increase in the size of mitochondria, their cristae and lipid drops in cytoplasm, the formation of more complicated configuration folding of plasmalemma and appearance of small-granular material of mean electron density in the periplasmic space of Chlorella cells grown during space flight, are demonstrated. Comparative cytological analysis has revealed general regularities of rearrangements of the submicroscopic organization in Chlorella cells cultivated on both solid and semiliquid agarized nutrient media.

Agar↗
PubMed2005

Quaternary assembly and crystal structure of GDP-D-mannose 4,6 dehydratase from Paramecium bursaria Chlorella virus.

GDP-D-mannose 4,6 dehydratase is the first enzyme in the de novo biosynthetic pathway of GDP-L-fucose, the activated form of L-fucose, a monosaccharide found in organisms ranging from bacteria to mammals. We determined the three-dimensional structure of GDP-D-mannose 4,6 dehydratase from the Paramecium bursaria Chlorella virus at 3.8A resolution. Unlike other viruses that use the host protein machinery to glycosylate their proteins, P. bursaria Chlorella virus modifies its structural proteins using many glycosyltransferases, being the first virus known to encode enzymes involved in sugar metabolism. P. bursaria Chlorella virus GDP-D-mannose 4,6 dehydratase belongs to the short-chain dehydrogenase/reductase protein superfamily. Accordingly, the family fold and the specific Thr, Tyr, and Lys catalytic triad are well conserved in the viral enzyme.

Animals↗