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  • Articles  (15)
  • Articles: DFG German National Licenses  (15)
  • 11
    Electronic Resource
    Electronic Resource
    Small subunit ribosomal RNA sequences of Phaeodarea challenge the monophyly of Haeckel's Radiolaria (2005)
    Oxford, UK : Blackwell Science Inc
    The @journal of eukaryotic microbiology 52 (2005), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In his grand monography of Radiolaria, Ernst Haeckel originally placed Phaeodarea within the class Radiolaria, together with Acantharea and Polycystinea. Cytological and ultrastructural studies, however, questioned the monophyly of Radiolaria, suggesting the independent evolutionary origin of the three taxa. Some recent molecular analyses based on small subunit ribosomal RNA (SSU rRNA) sequences challenged this classification, supporting the sisterhood of Acantharea and Polycystinea. In order to further test the monophyly of all Haeckel's Radiolaria, and as no data on Phaeodarea were available, we sequenced the complete SSU rRNA gene of three Phaeodarea and three Polycystinea. Our analyses show that the monophyletic Phaeodarea clearly branch among Cercozoa, and confirm that Acantharea and Polycystinea share a common history. This result enhances the morphological variability within Cercozoa, a phylum already containing very heterogeneous groups of protists. Our study suggests that the ability to secrete SrSO4 and the organization of microtubules inside axopodia are better phylogenetic markers than the simple presence of a central capsule and axopodia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2005.05202003_1_66.x
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  • 12
    Electronic Resource
    Electronic Resource
    Molecular Phylogenetic Analysis Places Percolomonas cosmopolites within Heterolobosea: Evolutionary Implications (2004)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 51 (2004), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Percolomonas cosmopolitus is a common free-living flagellate of uncertain phylogenetic position that was placed within the Heterolobosea on the basis of ultrastructure studies. To test the relationship between Percolomonas and Heterolobosea, we analysed the primary structure of the actin and small-subunit ribosomal RNA (SSU rRNA) genes of P. cosmopolitus as well as the predicted secondary structure of the SSU rRNA. Percolomonas shares common secondary structure patterns of the SSU rRNA with heterolobosean taxa, which, together with the results of actin gene analysis, confirms that it is closely related to Heterolobosea. Phylogenetic reconstructions based on the sequences of the SSU rRNA gene suggest Percolomonas belongs to the family Vahlkampliidae. The first Bayesian analysis of a large taxon sampling of heterolobosean SSU rRNA genes clarifies the phylogenetic relationships within this group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2004.tb00294.x
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  • 13
    Electronic Resource
    Electronic Resource
    Molecular Evidence That Reticulomyxa Filosa Is A Freshwater Naked Foraminifer (1999)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 46 (1999), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Reticulomyxa filosa is a freshwater protist possessing fine granular, branching and anastomosing pseudopodia and therefore traditionally placed in the class Granuloreticulosea, order Athalamida, as a sister group to the order Foraminiferida. Recent studies have revealed remarkable similarities in pseudopodial motility and ultrastructure between R. filosa and foraminifera (e.g. Allogromia laticollaris), prompting us to conduct a molecular phylogenetic analysis of these seemingly disparate organisms. We sequenced the complete small-subunit of the ribosomal DNA of the cultured strain of R. filosa and compared it to the corresponding sequences of other protists including 12 species of foraminifera. We also sequenced and analyzed the actin coding genes from R. filosa and two species of foraminifera, Allogromia sp. and Ammonia sp. the analysis of both data sets clearly shows that R. filosa branches within the clade of foraminifera, suggesting that R. filosa is in fact a freshwater naked foraminiferan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1999.tb05137.x
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  • 14
    Electronic Resource
    Electronic Resource
    Naked foraminiferans revealed (1999)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 399 (1999), S. 27-27 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] It is generally assumed that the first fossil appearance of a group of organisms corresponds to its evolutionary origin. But we have molecular evidence that extant members of the most abundant microfossil-forming group, the Foraminifera, include ‘naked’ amoeboid species, indicating ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/19881
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  • 15
    Electronic Resource
    Electronic Resource
    Actin in the ciliated protozoan Climacostomum virens: Purification by DNAse I affinity chromatography, electrophoretic characterization, and immunological analysis (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 22 (1992), S. 62-71 
    Details
    ISSN: 0886-1544
    Keywords: actin filaments ; actin isoforms ; anti-actin monoclonal antibodies ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The anti-actin monoclonal antibody (mab) JLA20 (Lin: Proc. Natl. Acad. Sci. U.S.A. 78:2335-2339, 1981) labels a 43 kD protein on Western blots of Climacostomum cell extracts; this protein does not react with an anti-α-smooth muscle actin mab (Skalli et al.: J. Cell Biol. 103:2787-2796, 1986) nor with an anti-α-sarcomeric actin mab (Skalli et al.: Am. J. Pathol. 130:515-531, 1988). This protein binds to DNAse I and can be purified by DNAse I affinity chromatography. The affinity-purified actin also reacts with mab JLA20. Two-dimensional gel analysis reveals that Climacostomum actin focuses as three spots which are more basic than the mammalian actin isoforms. After addition of KC1, the affinity-purified actin polymerizes into filaments as shown by electron microscopy after negative staining. © 1992 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970220107
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