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  • 1
    Electronic Resource
    Electronic Resource
    Evidence that Euglena chloroplasts do not export tRNAs (1979)
    [s.l.] : Nature Publishing Group
    Nature 280 (1979), S. 86-87 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] In our laboratory chloroplast-localised tRNAs of Euglena have been identified by Chromatographie comparisons with either total cellular tRNA or tRNA isolated from mutants lacking Chi DNA1. For each of 16 amino acids studied, isolated chloroplasts were found to contain unique Chromatographie species ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/280086a0
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  • 2
    Electronic Resource
    Electronic Resource
    Nutritional regulation of organelle biogenesis inEuglena: Photo- and metabolite induction of mitochondria (1980)
    Springer
    Planta 149 (1980), S. 376-383 
    Details
    ISSN: 1432-2048
    Keywords: Euglena ; Fumarase ; Light (mitochondria induction) ; Mitochondria ; Succinate dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Exposure of dark-grown restingEuglena gracilis Klebs var.bacillaris Cori to light, ethanol, or malate produced an increase in the specific activity of fumarase (EC. 4.2.1.2) and succinate dehydrogenase (EC. 1.3.99.1) during the first 8–12 h of exposure to inducer, followed by a decrease in the specific activity of both mitochondrial enzymes between 12 and 72 h. The increased specific activity represented a net increase in the level of active enzyme, and it was dependent upon cytoplasmic protein synthesis. The photoinduction of fumarase required continuous illumination while the subsequent decrease in fumarase specific activity was independent of light. Light had little effect on the ethanol and malate induction of fumarase and succinate dehydrogenase. In the mutant W3BUL, which has no detectable protochlorophyll(ide) and chloroplast DNA, light induced both mitochondrial enzymes and the kinetics of enzyme induction were similar to the induction kinetics in wild-type cells. The induction of mitochondrial enzymes appears to be controlled by a non-chloroplast photoreceptor. Dark-grown resting cells of the plastidless mutant W10SmL have lost the ability to regulate fumarase levels. In this mutant, the specific activity of fumarase fluctuated and light had little effect on these fluctuations, indicating that fumarase synthesis was uncoupled from the nonchloroplast photoreceptor. Ethanol addition produced transient changes in fumarase specific activity in W10SmL indicating that in this mutant, mitochondrial enzymes are still inductible by metabolites. Fumarase synthesis in wild-type cells was not induced in the dark by levulinic acid, a chemical inducer of the breakdown ofEuglena storage carbohydrates. Taken together, our results indicate that the photoinduction of mitochondrial enzyme synthesis is not a result of the photoinduction of carbohydrate breakdown. The mechanisms by which light and organic carbon induce the synthesis ofEuglena mitochondria may differ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00571173
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  • 3
    Electronic Resource
    Electronic Resource
    Photocontrol of the polypeptide composition ofEuglena (1983)
    Springer
    Planta 158 (1983), S. 249-258 
    Details
    ISSN: 1432-2048
    Keywords: Euglena ; Light and polypeptide synthesis ; Mutant (Euglena) ; Polypeptide coding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two-dimensional gel electrophoresis resolved total cellular protein fromEuglena gracilis Klebs var.bacillaris Cori into 650 polypeptides detectable by silver staining. Exposure of dark-grown restingEuglena to light for 72 h increased the relative amounts of 79 polypeptides and decreased the relative amounts of 72 polypeptides. Four polypeptides whose level increased upon light exposure were undetectable in the bleached mutant W3BUL. Since W3BUL has lost most if not all of its chloroplast genome, these polypeptides may be coded by the chloroplast genome. Although the majority of the polypeptides studied appear to be coded by the nuclear or mitochondrial genomes, seven polypeptides which were present in W3BUL were not detectable in another chloroplast-DNA-deficient, bleached mutant, W10BSmL. It appears that a number of nonchloroplast genes are no longer expressed in this mutant. Exposure of dark-grown resting cells of the bleached mutant, W3BUL, to light increased the relative amounts of 12 polypeptides and decreased the relative amounts of 14 polypeptides. Since W3BUL lacks detectable protochlorophyll(ide), the chloroplast photoreceptor, the levels of these polypeptides are regulated by light acting through a nonchloroplast photoreceptor. Exposure of cells to light had no detectable effect on the relative amounts of those polypeptides which were present in W10BSmL, even though W10BSmL has a nonchloroplast photoreceptor. EitherEuglena contains multiple nonchloroplast photoreceptors, some of which are absent from W10BSmL, or the nonchloroplast photoreceptor present in W10BSmL is uncoupled from some of the events normally controlled by that photoreceptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01075261
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  • 4
    Electronic Resource
    Electronic Resource
    Biosynthetic events required for lag elimination in chlorophyll synthesis in Euglena (1976)
    Springer
    Planta 131 (1976), S. 1-9 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Levulinic acid, a competitive inhibitor of δ aminolevulinic acid dehydratase, cycloheximide, an inhibitor of translation on 89s cytoplasmic ribosomes, and chloramphenicol, an inhibitor of translation on 68s chloroplast ribosomes, are reversible inhibitors of light induced chlorophyll synthesis in resting Euglena gracilis Klebs. When dark grown resting cells are preilluminated for 2 h followed by darkness for 12 h prior to exposure to continuous light, the usual lag period in chlorophyll formation is eliminated. If cycloheximide, chloramphenicol, or levulinic acid are present during either the preillumination period or the subsequent dark period, the lag is reestablished. Only the very beginning of the dark period is sensitive to cycloheximide but the dark period is less sensitive to levulinic acid than is the light period. Exposure of preilluminated cells to cycloheximide or levulinic acid at the time of exposure to continuous illumination completely inhibits chlorophyll synthesis indicating that the potential for rapid chlorophyll synthesis generated by preillumination and a dark period does not result simply from the accumulation of porphyrin precursors. Preillumination has little effect on the development of the capacity to fix CO2 photosynthetically. These results indicate that the control of chlorophyll formation is more complex than in higher plants and a model based on the formation of certain crucial enzymes in the porphyrin pathway, rather than simply upon the accumulation of δ aminolevulinic acid is presented to explain the experimental findings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00387337
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  • 5
    Electronic Resource
    Electronic Resource
    Photo and nutritional regulation of chloroplast valyl-tRNA synthetase in Euglena (1982)
    Springer
    Archives of microbiology 133 (1982), S. 149-154 
    Details
    ISSN: 1432-072X
    Keywords: Euglena gracilis ; Strain W3BUL, Strain W10BSmL ; Chloroplast valyl-tRNA synthetase ; Photoinduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Exposure of dark grown resting Euglena to light induced the synthesis of chloroplast valyl-tRNA synthetase. Ethanol, a specific inhibitor of Euglena chloroplast development had little effect on chloroplast valyl-tRNA synthetase induction during the first 12 h of light exposure. Ethanol, however, completely inhibited enzyme synthesis between 12–72 h of light exposure. Malate, an alternative carbon source, had little effect on the photoinduction of valyl-tRNA synthetase. When dark grown resting cells were exposed to 2 h of light and returned to the dark, chloroplast valyl-tRNA synthetase continued to accumulate for 8–12 h at a rate which was less than the rate in cells maintained continuously in the light. The mutant strain W3BUL lacks detectable chloroplast DNA and phototransformable protochlorophyllide, but retains a plastid remnant. Exposure of strain W3BUL to light induced the synthesis of chloroplast valyl-tRNA synthetase and enzyme induction was not inhibited by ethanol. After 72 h of light exposure in the presence or absence of ethanol, enzyme levels in strain W3BUL were comparable to the levels found in the wildtype strain after 8–14 h of light exposure. These results suggest that the nonchloroplast photoreceptor regulates the initial phase of enzyme synthesis. Mutant strain W10BSmL differs from strain W3BUL in that the plastid remnant if present, is greatly reduced. Chloroplast valyl-tRNA synthetase was undetectable in the strain W10BSmL suggesting that the levels of active, cytoplasmically synthesized, chloroplast localized enzymes may be related to the developmental status of the chloroplast through the extent to which the enzyme precursor can be accumulated and or posttranslationally processed into an active enzyme within the chloroplast or chloroplast remnant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00413530
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of a Euglena gene encoding a polyprotein precursor to the light-harvesting chlorophyll a/b-binding protein of photosystem II (1992)
    Springer
    Plant molecular biology 18 (1992), S. 287-299 
    Details
    ISSN: 1573-5028
    Keywords: Euglena ; intron-exon junctions ; LHCPII ; polyprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 7.4 kb segment of a Euglena nuclear gene encoding a portion of the polyprotein precursor to the light-harvesting chlorophyll a/b-binding protein of photosystem II (LHCPII) has been isolated and sequenced. Nine exons can be assembled into a continuous open reading frame encoding 113 amino acids of the C-terminus of an LHCPII, followed by 4 complete LHCPIIs. The intron-exon junctions required to maintain maximum amino acid sequence homology between the LHCPIIs encoded by the Euglena genomic clone and Arabidopsis LHCPII do not conform to the consensus splice site sequences present in most eukaryotic organisms. Three types of LHCPIIs are contained within the polyprotein precursor. There is greater than 90% sequence identity at both the protein and nucleic acid level within a type while between types, there is less than 65% sequence identity. All Euglena LHCPIIs contain three hydrophobic membrane-spanning domains in the same positions as found in other LHCPIIs. Hybridization of genomic Southern blots with a probe encoding LHCPII suggests that the Euglena genome encodes a large number (30–50) of LHCPIIs. A probe derived from the 3′ end of the sequenced genomic clone hybridizes with equal intensity to 2–3 genomic fragments on Southern blots. The probe encoding LHCPII hybridizes to RNAs of 9.5 and 6.6 kb on northern blots of total RNA while the 3′-end probe hybridizes only to the 6.6 kb RNA. The 6.6 kb LHCPII band detected on northern blots appears to be composed of transcription products derived from 2–3 LHCPII genes. Euglena appears to be unique in that a large number of LHCPIIs are encoded by a small number (3–5) of polyprotein genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00034956
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  • 7
    Electronic Resource
    Electronic Resource
    Regulation by light and ethanol of the synthesis of the light-harvesting chlorophyll a/b-binding protein of photosystem II in Euglena (1989)
    Springer
    Planta 178 (1989), S. 76-83 
    Details
    ISSN: 1432-2048
    Keywords: Chloroplast biogenesis ; Euglena ; Light and gene expression ; Light-harvesting chlorophyll a/b-binding protein of photosystem II
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In dark-grown Euglena, a single 122-kdalton (kDa) precursor to the light-harvesting chlorophyll a/b-binding protein of photosystem II (pLHCPII) was synthesized at a very low rate and LHCPII synthesis was undetectable as determined by pulse-labeling with [35S]sulfate and immunoprecipitation with a specific antibody against Euglena LHCPII. Synthesis of a 207-, 161-, 122- and 110-kDa pLHCPII was detected after light exposure, with the 207-kDa pLHCPII being the most abundant pLHCPII synthesized. The rate of synthesis of all four pLHCPIIs and the 25.6-kDa and 27.2-kDa LHCPIIs increased in the first 12–24 h of light exposure and then declined. The maximal rate of LHCPII synthesis in the light was 50–100-fold greater than the rate in darkness. Addition of ethanol at the time of light exposure inhibited LHCPII synthesis, indicating that induction is catabolite-sensitive. The halflife of pLHCPII in the light or in darkness was 20 min. Therefore, the light induction of LHCPII is the result of an increased rate of synthesis rather than a decreased rate of degradation. Transfer of illuminated cells to darkness resulted in an 80% decrease in the rate of pHLCPII synthesis during the first 0.5 h. Illuminated cells returned to darkness continued to synthesize both 207-kDa pLHCPII and LHCPII for at least 5 h. Light exposure or ethanol addition did not increase the level of translatable RNA for LHCPII. The 50–100-fold catabolite-sensitive increase in the rate of LHCPII synthesis in the absence of a concomitant increase in the level of translatable RNA for LHCPII indicates that in Euglena, the synthesis of LHCPII is controlled at the translational rather than at the transcriptional level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392529
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  • 8
    Electronic Resource
    Electronic Resource
    Organization of the chloroplast ribosomal RNA genes of Euglena gracilis bacillaris (1979)
    Springer
    Molecular genetics and genomics 174 (1979), S. 1-10 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The order of eight of the 29 endonuclease EcoRI-generated fragments of chloroplast DNA was determined. Three sets of rRNA genes aligned sequentially in the same orientation form part of this region. The repeated sets differ in the length and sequence of the spacers among themselves and with the rRNA genes of E. gracilis strain Z.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00433298
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  • 9
    Electronic Resource
    Electronic Resource
    Protein import into cyanelles and complex chloroplasts (1998)
    Springer
    Plant molecular biology 38 (1998), S. 247-263 
    Details
    ISSN: 1573-5028
    Keywords: cyanelles ; dinoflagellates ; Euglena ; red algae ; chromophytes ; protein import
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Higher-plant, green and red algal chloroplasts are surrounded by a double membrane envelope. The glaucocystophyte plastid (cyanelle) has retained a prokaryotic cell wall between the two envelope membranes. The complex chloroplasts of Euglena and dinoflagellates are surrounded by three membranes while the complex chloroplasts of chlorarachniophytes, cryptomonads, brown algae, diatoms and other chromophytes, are surrounded by 4 membranes. The peptidoglycan layer of the cyanelle envelope and the additional membranes of complex chloroplasts provide barriers to chloroplast protein import not present in the simpler double membrane chloroplast envelope. Analysis of presequence structure and in vitro import experiments indicate that proteins are imported directly from the cytoplasm across the two envelope membranes and peptidoglycan layer into cyanelles. Protein import into complex chloroplasts is however fundamentally different. Analysis of presequence structure and in vitro import into microsomal membranes has shown that translocation into the ER is the first step for protein import into complex chloroplasts enclosed by three or four membranes. In vivo pulse chase experiments and immunoelectronmicroscopy have shown that in Euglena, proteins are transported from the ER to the Golgi apparatus prior to import across the three chloroplast membranes. Ultrastructural studies and the presence of ribosomes on the outermost of the four envelope membranes suggests protein import into 4 membrane-bounded complex chloroplasts is directly from the ER like outermost membrane into the chloroplast. The fundamental difference in import mechanisms, post-translational direct chloroplast import or co-translational translocation into the ER prior to chloroplast import, appears to reflect the evolutionary origin of the different chloroplast types. Chloroplasts with a two-membrane envelope are thought to have evolved through the primary endosymbiotic association between a eukaryotic host and a photosynthetic prokaryote while complex chloroplasts are believed to have evolved through a secondary endosymbiotic association between a heterotrophic or possibly phototrophic eukaryotic host and a photosynthetic eukaryote.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006029919283
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  • 10
    Electronic Resource
    Electronic Resource
    Photocontrol of organelle and cell type specific changes in the polypeptide composition of Euglena and sorghum (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 764-773 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two-dimensional (2-D) gel electrophoresis has been used to follow changes in cell type specific and organelle localized polypeptides upon exposure of etiolated sorghum shoots and dark-grown resting Euglena to light. Total protein extracted from isolated bundle sheath strands and mesophyll protoplasts was resolved by 2-D gel electrophoresis. The cell type specific polypeptides were localized on the whole shoot 2-D gel map in order to determine changes in the levels of these polypeptides upon light exposure. An image analyzer was used to analyze fluorographs of 2-D gels of total Euglena protein pulse-labeled with [35S]sulfate in the dark, immediately upon light exposure and 1, 4, 14, 24, 48 and 72 h after light exposure. The subset of polypeptides whose relative rats of synthesis changes more than threefold immediately upon light exposure was i dentified. The different patterns of changes in the rate of synthesis of this subset of polypeptides were followed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150091112
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