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  • 1
    ISSN: 1432-1432
    Keywords: Cyanelles ; Cyanophora paradoxa ; Endosymbiosis ; Evolution ; Glaucocystophyta ; Glaucophyta ; Phylogeny ; Plastid ; 16S ribosomal RNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glaucocystophyte algae (sensu Kies, Berl. Deutsch. Bot. Ges. 92, 1979) contain plastids (cyanelles) that retain the peptidoglycan wall of the putative cyanobacterial endosymbiont; this and other ultrastructural characters (e.g., unstacked thylakoids, phycobilisomes) have suggested that cyanelles are “primitive” plastids that may represent undeveloped associations between heterotrophic “host” cells (i.e., glaucocystophytes) and cyanobacteria. To test the monophyly of glaucocystophyte cyanelles and to determine their evolutionary relationship to other plastids, complete 16S ribosomal RNA sequences were determined for Cyanophora paradoxa, Glaucocystis nostochinearum, Glaucosphaera vacuolata, and Gloeochaete wittrockiana. Plastid rRNAs were analyzed with the maximum-likelihood, maximumparsimony, and neighbor joining methods. The phylogenetic analyses show that the cyanelles of C. paradoxa, G. nostochinearum, and G. wittrockiana form a distinct evolutionary lineage; these cyanelles presumably share a monophyletic origin. The rDNA sequence of G. vacuolata was positioned within the nongreen plastid lineage. This result is consistent with analyses of nuclear-encoded rRNAs that identify G. vacuolata as a rhodophyte and support its removal from the Glaucocystophyta. Results of a global search with the maximumlikelihood method suggest that cyanelles are the first divergence among all plastids; this result is consistent with a single loss of the peptidoglycan wall in plastids after the divergence of the cyanelles. User-defined tree analyses with the maximum-likelihood method indicate, however, that the position of the cyanelles is not stable within the rRNA phylogenies. Both maximumparsimony and neighbor-joining analyses showed a close evolutionary relationship between cyanelles and nongreen plastids; these phylogenetic methods were sensitive to inclusion/exclusion of the G. wittrockiana cyanelle sequence. Base compositional bias within the G. wittrockiana 16S rRNA may explain this result. Taken together the phylogenetic analyses are interpreted as supporting a near-simultaneous radiation of cyanelles and green and nongreen plastids; these organelles are all rooted within the cyanobacteria.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 135 (1983), S. 25-29 
    ISSN: 1432-072X
    Keywords: Electron microscopy ; Euglena mutabilis ; Flagellate ; Photomovement ; Photoreceptor ; Phototaxis ; Single-cell analysis ; Videomicroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Due to the lack of an emergent flagellum the green flagellate Euglena mutabilis is restricted to gliding motility. During forward movement, the organisms orient positive phototactically in the presence of a suitable light stimulus. The cell contains both a stigma and a paraflagellar body which differ in shape and size from the organelles found in E. gracilis. The degree of orientation in white light follows an optimum curve with a maximum at about 100 lx. The spectral sensitivity shows a number of prominent peaks in the blue and green regions and extends well into the red region of the visible spectrum. Since the cell does not rotate during locomotion a periodic shading mechanism cannot account for phototactic orientation. Thus, phototaxis in the related species, E. gracilis and E. mutabilis differ in their photoreceptor molecules, their sensory transduction chains and their strategies of light direction detection.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0983
    Keywords: Key words  Group-I introns ; Secondary structure ; Small subunit ribosomal DNA ; Zygnematales
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract   The Zygnematales (Charophyta) contain a group-I intron (subgroup IC1) within their nuclear-encoded small subunit ribosomal DNA (SSU rDNA) coding region. This intron, which is inserted after position 1506 (relative to the SSU rDNA of Escherichia coli), is proposed to have been vertically inherited since the origin of the Zygnematales approximately 350–400 million years ago. Primary and secondary structure analyses were carried out to model group-I intron evolution in the Zygnematales. Secondary structure analyses support genetic data regarding sequence conservation within regions known to be functionally important for in vitro self-splicing of group-I introns. Comparisons of zygnematalean group-I intron secondary structures also provided some new insights into sequences that may have important roles in in vivo RNA splicing. Sequence analyses showed that sequence divergence rates and the nucleotide compositions of introns and coding regions within any one taxon varied widely, suggesting that the ``1506'' group-I introns and rDNA coding regions in the Zygnematales evolve independently.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0983
    Keywords: Group-I introns ; Secondary structure ; Small subunit ribosomal DNA ; Zygnematales
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Zygnematales (Charophyta) contain a group-I intron (subgroup ICl) within their nuclear-encoded small subunit ribosomal DNA (SSU rDNA) coding region. This intron, which is inserted after position 1506 (relative to the SSU rDNA ofEscherichia coli), is proposed to have been vertically inherited since the origin of the Zygnematales approximately 350–400 million years ago. Primary and secondary structure analyses were carried out to model group-I intron evolution in the Zygnematales. Secondary structure analyses support genetic data regarding sequence conservation within regions known to be functionally important for in vitro self-splicing of group-I introns. Comparisons of zygnematalean group-I intron secondary structures also provided some new insights into sequences that may have important roles in in vivo RNA splicing. Sequence analyses showed that sequence divergence rates and the nucleotide compositions of introns and coding regions within any one taxon varied widely, suggesting that the “1506” group-I introns and rDNA coding regions in the Zygnematales evolve independently.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The Rhizopoda comprise a diverse assemblage of protists which depend on lobose or filose pseudopodia for locomotion. The biochemical and morphological diversity of rhizopods has led to an uncertain taxonomy. Ribosomal RNA sequence comparisons offer a measure of evolutionary relatedness that is independent of morphology and has been used to demonstrate a polyphyletic origin of the Lobosea. We sequenced complete small subunit ribosomal RNA coding regions from the filose amoebae, Euglypha rotunda and Paulinella chromatophora (Euglyphina) to position these taxa in the eukaryote phylogeny. The neighbor-joining analyses show that E. rotunda and P. chromatophora share a monophyletic origin and are not closely related to any lobose amoebae in our analyses. Instead, the Euglyphina form a robust sister group to the Chlorarachniophyta. These results provide further evidence for the polyphyly of the Rhizopoda and support the creation of a new amoeboid lineage which includes the Euglyphina and the chlorarachniophyte algae; taxa with tubular mitochondrial cristae and filose or reticulate pseudopodia.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 34 (1987), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An account of the fine structure of Vampyrellidium perforans is given. The organism has filose pseudopodia, mitochondria with flattened cristae, and cytoplasmic microtubules, some of which arise from a perinuclear cytoplasmic sheath. Microtubules were observed within nuclei presumed to be at an early stage of division. Relatively massive (non-filose) pseudopodia are formed by cells feeding by engulfment. The cytoplasm of these pseudopodia has a fibrillar consistency with local aggregations of material. Despite sharing aspects of feeding behavior with vampyrellid filose amoebae, Vampyrellidium perforans is ultrastructurally more similar to Nuclearia, and it is here assigned to nucleariid filose amoebae.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 66 (1986), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: α-1,4-Glucan phosphorylase (EC 2.4.1.1) forms from light or dark grown shoots of Pisum sativum L. cv. ‘Kleine Rheinländerin’ have been studied using various electrophoretic techniques. The phosphorylase patterns of green and etiolated shoots differed. Etiolated shoots contained two enzyme forms, one residing inside and the other outside the etioplast; this was shown by electrophoresis of extracts of isolated etioplasts. Purity and intactness of the organelle preparation were ascertained by electron microscopy. Light-grown shoots contained, in addition to these two enzyme forms, a third phosphorylase which appears to be chloroplast-specific. The two plastidic phosphorylase forms differed slightly in their apparent molecular masses (as determined by non-denaturing polyacrylamide gel electrophoresis) and in their affinities towards branched polyglucans (as revealed by affinity electrophoresis). The apparent affinity of the extrachloroplastic phosphorylase form to these polyglucans was orders of magnitude higher than that of the two plastidic enzyme forms. The development of the chloroplast-specific phosphorylase pattern is under photocontrol. Investigations performed with red or far-red illuminated wild-type plants and with a pale mutant which has a highly reduced pigment and thylakoid content suggest that this photocontrol is mediated by phytochrome.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 51 (1981), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In extracts of the unicellular green alga Eremosphaera viridis DeBary (Chlorococcales, Chlorophyceae) the average specific activity of α-1,4-glucan phosphorylase (E.C. 2.4.1.1) was 200 nmol glucose 1-phosphate formed per min and mg protein. Using continuous and discontinuous electrophoresis on polyacrylamide gels, three phosphorylase forms were found. When the log of the relative mobility of the three enzyme forms was plotted versus the acrylamide gel concentration (Ferguson plot) parallel lines were obtained, indicating that the three enzymes were indiscernible with respect to molecular weight. Electrophoresis on density gradient gels resulted in three activity zones lying close to each other. The relative molecular mass (Mr) of the three enzymes was estimated to be around 180,000 with a difference of less than 7,000 between the small and the large forms.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-2048
    Keywords: Flagellar membrane ; Glycoprotein immunolocalization ; Lectin ; Scale ; Scherffelia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Flagellar scales were isolated from the flagellate green alga Scherffelia dubia. The flagellar scales consist mainly of acidic polysaccharides (70%) and glycoproteins (10%), and monosaccharide analyses show that the scales contain high amounts of unusual 2-keto-sugar acids. Approximately, 72 mol% of total carbohydrate is 3-deoxy-manno-2-octulosonic acid, 3-deoxy-5-O-methylmanno-2-octulosonic acid and 3-deoxy-lyxo-2-heptulosaric acid. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed the presence of at least 18 different scale-associated proteins (SAPs), ranging in apparent molecular mass from 77 kDa to over 300 kDa. Lectin blot analyses performed in combination with glycosidase treatment, showed that SAPs contained N-glycans of the highmannose type and the hybrid type, as well as a complex type that was not immunologically related to higher-plant complex glycans. Most of the SAPs were present in two or possibly three high-molecular-weight complexes. In these complexes, individual polypeptides are cross-linked by disulfide bridges. A polyclonal antibody was raised against a SAP of 126 kDa (SAP 126), a glycoprotein present in a high-molecular-weight complex. The SAP126 antibody was used to localize the protein between scale layer and flagellar membrane. We suggest that these high-molecular-weight complexes link scales to the flagellar membrane.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-2048
    Keywords: Key words: cytokinin – Cytokinin conjugate –β-Glucosidase – Immunolocalization –Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A β-glucosidase that cleaves the biologically inactive hormone conjugates cytokinin-O- and kinetin-N3-glucosides is encoded by the maize Zm-p60.1 gene. The expression of the Zm-p60.1 gene was analyzed by Northern blot analysis and in-situ hybridization. It was found that the expression levels of the Zm-p60.1-specific mRNA changed after pollination of carpellate inflorescences. The Zm-p60.1 cDNA was expressed in E. coli and antibodies were raised against this protein. An antibody was used to determine the tissue-specific localization of this protein. By in situ immunolocalization experiments, this protein was found to be located in cell layers below the epidermis and around the vascular bundles of the coleoptile. In the primary leaf, the Zm-p60.1 protein was detected in cells of the outermost cell layer and around the vascular tissue. In floral tissue, Zm-p60.1 was present in the glumes, the carpels and in the outer cell layer of the style. In coleoptiles, as determined by immuno-electronmicroscopy, the Zm-p60.1 protein was located exclusively in the plastids.
    Type of Medium: Electronic Resource
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