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  • 1
    Online Resource
    Online Resource
    Anaerobic Parasitic Protozoa : Genomics and Molecular Biology. (2010)
    Norfolk :Caister Academic Press,
    Details
    Keywords: Anaerobic protozoa-Genetics. ; Electronic books.
    Description / Table of Contents: In this book internationally acclaimed researchers critically review the most important aspects of research on anaerobic parasitic protozoa, providing the first coherent picture of their genomics and molecular biology since the publication of the genomes. Chapters are written from a molecular and genomic perspective and contain speculative models upon which future research efforts can be based. Topics include: the genomes of Entamoeba histolytica, Trichomonas vaginalis, Giardia and other diplomonads; the cytoskeletons of Entamoeba histolytica, Giardia lamblia and Trichomonas vaginalis; genomic analyses and manipulation of gene expression in Entamoeba histolytica; nuclear and chromosomal structure and replication in Giardia; and the mitochondrion-like organelles of a fourth anaerobe, Blastocystis. Essential reading for all researchers working with these protozoa and related organisms and with eukaryotic model organisms. Recommended text for all parasitology laboratories.
    Type of Medium: Online Resource
    Pages: 1 online resource (234 pages)
    Edition: 1st ed.
    ISBN: 9781912530861
    URL: https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=6122001
    DDC: 616.96
    Language: English
    Note: Intro -- Contents -- 1 -- 2 -- 3 -- 4 -- 5 -- 6 -- 7 -- 8 -- 9 -- Index.
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  • 2
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    Proteins of the glycine decarboxylase complex in the Hydrogenosome of Trichomonas vaginalis (2007)
    American Society for Microbiology
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © American Society for Microbiology, 2006. This article is posted here by permission of American Society for Microbiology for personal use, not for redistribution. The definitive version was published in Eukaryotic Cell 5 (2006): 2062-2071, doi:10.1128/EC.00205-06.
    Description: Trichomonas vaginalis is a unicellular eukaryote that lacks mitochondria and contains a specialized organelle, the hydrogenosome, involved in carbohydrate metabolism and iron-sulfur cluster assembly. We report the identification of two glycine cleavage H proteins and a dihydrolipoamide dehydrogenase (L protein) of the glycine decarboxylase complex in T. vaginalis with predicted N-terminal hydrogenosomal presequences. Immunofluorescence analyses reveal that both H and L proteins are localized in hydrogenosomes, providing the first evidence for amino acid metabolism in this organelle. All three proteins were expressed in Escherichia coli and purified to homogeneity. The experimental Km of L protein for the two H proteins were 2.6 µM and 3.7 µM, consistent with both H proteins serving as substrates of L protein. Analyses using purified hydrogenosomes showed that endogenous H proteins exist as monomers and endogenous L protein as a homodimer in their native states. Phylogenetic analyses of L proteins revealed that the T. vaginalis homologue shares a common ancestry with dihydrolipoamide dehydrogenases from the firmicute bacteria, indicating its acquisition via a horizontal gene transfer event independent of the origins of mitochondria and hydrogenosomes.
    Description: This work was supported by National Institutes of Health (NIH) grants to P.J.J., a Burroughs-Wellcome Molecular Parasitology Award to P.J.J., and an NIH Microbial Pathogenesis Training Grant (2-T32-AI-07323) to M.T.B. A.G.M. was supported by the Marine Biological Laboratory's Program in Global Infectious Disease, funded by the Ellison Medical Foundation.
    Repository Name: Woods Hole Open Access Server
    Type: Article
    Format: 3312882 bytes
    Format: application/pdf
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    PAPER (OA)
  • 3
    Electronic Resource
    Electronic Resource
    Targeted gene replacement of a ferredoxin gene in Trichomonas vaginalis does not lead to metronidazole resistance (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 51 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Ferredoxin, Fd, is often deficient in metronidazole-resistant strains of Trichomonas vaginalis and is thought to be necessary for drug activation. To directly test whether Fd is essential for metronidazole susceptibility, gene replacement technology has been developed for T. vaginalis. The selectable marker gene neomycin phosphotransferase (NEO) flanked by ∼2.6 and ∼2.0 kBp of the Fd 5′ and 3′ flanking regions (pKO-FD-NEO) was introduced into cells on linear DNA and selected for NEO gene expression. Stable transformants were shown to contain the NEO gene in the Fd locus and to have completely lost the Fd gene. Northern and immunoblot analyses confirm the loss of Fd mRNA and protein in pKO-FD-NEO cells. Analyses of the activity of hydrogenosomal proteins in Fd KO cells show a fourfold increase in hydrogenase activity and a 95% decrease in pyruvate/ferredoxin oxidoreductase (PFO) activity. In contrast, PFO and hydrogenase mRNA levels are unchanged. Surprisingly, Fd KO cells are not resistant to metronidazole under aerobic or anaerobic conditions. These cells are capable of producing molecular hydrogen, albeit at 50% the level of the parental strain, demonstrating that the Fd gene product eliminated in KO cells is neither necessary for hydrogen production nor metronidazole activation. Together these data indicate the presence of unidentified Fds or flavodoxins capable of drug activation or an unidentified mechanism that does not require either PFO or Fd for metronidazole activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03791.x
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  • 4
    Electronic Resource
    Electronic Resource
    Ellobiopsids of the Genus Thalassomyces are Alveolates (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: . Ellobiopsids are multinucleate protist parasites of aquatic crustaceans that possess a nutrient absorbing ‘root’ inside the host and reproductive structures that protrude through the carapace. Ellobiopsids have variously been affiliated with fungi, ‘colorless algae’, and dinoflagellates, although no morphological character has been identified that definitively alh'es them with any particular eukaryotic lineage. The arrangement of the trailing and circumferential flagella of the rarely observed bi-flagellated ‘zoospore’ is reminiscent of dinoflagellate flagellation, but a well-organized ‘dinokaryotic nucleus’ has never been observed. Using small subunit ribosomal RNA gene sequences from two species of Thalassomyces, phylogenetic analyses robustly place these ellobiopsid species among the alveolates (ciliates, apicomplexans, dinoflagellates and relatives) though without a clear affiliation to any established alveolate lineage. Our trees demonstrate that Thalassomyces fall within a dinoflagellate + apicomplexa + Perkinsidae +“marine alveolate group 1” clade, clustering most closely with dinoflagellates. However, the poor statistical support for branches within this region indicates that additional data will be needed to resolve relationships among these taxa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2004.tb00555.x
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  • 5
    Electronic Resource
    Electronic Resource
    Non-mitochondrial complex I proteins in a hydrogenosomal oxidoreductase complex (2004)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 431 (2004), S. 1103-1107 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Trichomonas vaginalis is a unicellular microaerophilic eukaryote that lacks mitochondria yet contains an alternative organelle, the hydrogenosome, involved in pyruvate metabolism. Pathways between the two organelles differ substantially: in hydrogenosomes, pyruvate oxidation is catalysed by ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature02990
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  • 6
    Electronic Resource
    Electronic Resource
    Transcription in the Early Diverging Eukaryote Trichomonas vaginalis: An Unusual RNA Polymerase II and α-Amanitin–Resistant Transcription of Protein-Coding Genes (1996)
    Springer
    Journal of molecular evolution 43 (1996), S. 253-262 
    Details
    ISSN: 1432-1432
    Keywords: Key words:α-Amanitin-resistant transcription — RNA polymerase II — Early diverging eukaryote —Trichomonas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. We have examined transcription in an early diverging eukaryote by analyzing the effect of the fungus-derived toxin α-amanitin on the transcription of protein-coding genes of the protist Trichomonas vaginalis. In contrast to that typical in eukaryotes, the RNA polymerase that transcribes T. vaginalis protein-coding genes is relatively resistant to α-amanitin (50% inhibition = 250 μg α-amanitin/ml). We have also characterized the gene encoding the largest subunit of RNA polymerase II, the subunit that binds α-amanitin. This protein is 41% identical to the mouse RNA polymerase II. Sequence analysis of the 50-amino-acid region thought to bind α-amanitin shows that this region of the trichomonad RNA polymerase II lacks many of the conserved amino acids present in the putative binding site, in agreement with the observed insensitivity to this inhibitor. Similar to other RNA polymerase IIs analyzed from ancient eukaryotes, the T. vaginalis RNA polymerase II lacks the typical heptapeptide (Tyr-Ser-Pro-Thr-Ser-Pro-Ser) repeat carboxyl-terminal domain (CTD) that is a hallmark of higher eukaryotic RNA polymerase IIs. The trichomonad enzyme, however, does contain a short modified CTD that is rich in the amino acid residues that compose the repeat. These data suggest that T. vaginalis protein-coding genes are transcribed by a RNA polymerase II that is relatively insensitive to α-amanitin and that differs from typical eukaryotic RNA polymerase IIs as it lacks a heptapeptide repeated CTD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00006084
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  • 7
    Electronic Resource
    Electronic Resource
    The Sequence and Organization of the Core Histone H3 and H4 Genes in the Early Branching Amitochondriate Protist Trichomonas vaginalis (1996)
    Springer
    Journal of molecular evolution 43 (1996), S. 563-571 
    Details
    ISSN: 1432-1432
    Keywords: Key words: Histone — Amitochondriate protist —Trichomonas vaginalis— Protein evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Among the unicellular protists, several of which are parasitic, some of the most divergent eukaryotic species are found. The evolutionary distances between protists are so large that even slowly evolving proteins like histones are strongly divergent. In this study we isolated cDNA and genomic histone H3 and H4 clones from Trichomonas vaginalis. Two histone H3 and three histone H4 genes were detected on three genomic clones with one complete H3 and two complete H4 sequences. H3 and H4 genes were divergently transcribed with very short intergenic regions of only 194 bp, which contained T. vaginalis-specific as well as histone-specific putative promoter elements. Southern blot analysis showed that there may be several more histone gene pairs. The two complete histone H4 genes were different on the nucleotide level but encoded the same amino acid sequence. Comparison of the amino acid sequences of the T. vaginalis H3 and H4 histones with sequences from animals, fungi, and plants as well as other protists revealed a significant divergence not only from the sequences in multicellular organisms but especially from the sequences in other protists like Entamoeba histolytica, Trypanosoma cruzi, and Leishmania infantum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02202104
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  • 8
    Electronic Resource
    Electronic Resource
    The sequence and organization of the core histone H3 and H4 genes in the early branching amitochondriate protistTrichomonas vaginalis (1996)
    Springer
    Journal of molecular evolution 43 (1996), S. 563-571 
    Details
    ISSN: 1432-1432
    Keywords: Histone ; Amitochondriate protist ; Trichomonas vaginalis ; Protein evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Among the unicellular protists, several of which are parasitic, some of the most divergent eukaryotic species are found. The evolutionary distances between protists are so large that even slowly evolving proteins like histones are strongly divergent. In this study we isolated cDNA and genomic histone H3 and H4 clones fromTrichomonas vaginalis. Two histone H3 and three histone H4 genes were detected on three genomic clones with one complete H3 and two complete H4 sequences. H3 and H4 genes were divergently transcribed with very short intergenic regions of only 194 bp, which containedT. vaginalis-specific as well as histone-specific putative promoter elements. Southern blot analysis showed that there may be several more histone gene pairs. The two complete histone H4 genes were different on the nucleotide level but encoded the same amino acid sequence. Comparison of the amino acid sequences of theT. vaginalis H3 and H4 histones with sequences from animals, fungi, and plants as well as other protists revealed a significant divergence not only from the sequences in multicellular organisms but especially from the sequences in other protists likeEntamoeba histolytica, Trypanosoma cruzi, andLeishmania infantum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02202104
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    Paper (German National Licenses)
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  • 9
    Electronic Resource
    Electronic Resource
    Transcription in the early diverging eukaryoteTrichomonas vaginalis: An unusual RNA polymerase II and α-amanitin-resistant transcription of protein-coding genes (1996)
    Springer
    Journal of molecular evolution 43 (1996), S. 253-262 
    Details
    ISSN: 1432-1432
    Keywords: α-Amanitin-resistant transcription ; RNA polymerase II ; Early diverging eukaryote ; Trichomonas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have examined transcription in an early diverging eukaryote by analyzing the effect of the fungus-derived toxin α-amanitin on the transcription of protein-coding genes of the protistTrichomonas vaginalis. In contrast to that typical in eukaryotes, the RNA polymerase that transcribesT. vaginalis protein-coding genes is relatively resistant to α-amanitin (50% inhibition = 250 μg α-amanitin/ml). We have also characterized the gene encoding the largest subunit of RNA polymerase II, the subunit that binds α-amanitin. This protein is 41% identical to the mouse RNA polymerase II. Sequence analysis of the 50-amino-acid region thought to bind α-amanitin shows that this region of the trichomonad RNA polymerase II lacks many of the conserved amino acids present in the putative binding site, in agreement with the observed insensitivity to this inhibitor. Similar to other RNA polymerase Its analyzed from ancient eukaryotes, theT. vaginalis RNA polymerase II lacks the typical heptapeptide (Tyr-Ser-Pro-Thr-Ser-Pro-Ser) repeat carboxyl-terminal domain (CTD) that is a hallmark of higher eukaryotic RNA polymerase IIs. The trichomonad enzyme, however, does contain a short modified CTD that is rich in the amino acid residues that compose the repeat. These data suggest thatT. vaginalis protein-coding genes are transcribed by a RNA polymerase II that is relatively insensitive to α-amanitin and that differs from typical eukaryotic RNA polymerase Its as it lacks a heptapeptide repeated CTD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02338833
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  • 10
    Electronic Resource
    Electronic Resource
    Evolution of two actin genes in the sea urchinStrongylocentrotus franciscanus (1985)
    Springer
    Journal of molecular evolution 22 (1985), S. 108-116 
    Details
    ISSN: 1432-1432
    Keywords: Actin ; DNA divergence ; Gene duplication ; Strongylocentrotus franciscanus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The complete nucleotide sequences of two chromosomally linked actin genes from the sea urchinStrongylocentrotus franciscanus are presented. The genes are separated by 5.7 kilobases, occur in the same transcriptional orientation, and contain introns in identical positions. The structures and nucleotide sequences of the two genes are extremely similar, suggesting that they arose through a recent duplication. Comparison of the nucleotide sequences of the genes allows inferences to be made about mutational mechanisms active since the duplication event. Whereas point mutations predominate in the coding regions, the introns and flanking DNA are more heavily influenced by a variety of events that cause simultaneous changes in short regions of DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02101689
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