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  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Eukaryotic cells. ; Eukaryotic cells -- Evolution. ; Mitochondria. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (320 pages)
    Edition: 1st ed.
    ISBN: 9783540385028
    DDC: 571.6
    Language: English
    Note: Intro -- CONTENTS -- The Road to Hydrogenosomes -- 1.1 Introduction -- 1.2 The Story -- 1.3 Conclusion -- References -- 2 Mitochondria: Key to Complexity -- 2.1 Introduction -- 2.2 Size -- 2.3 Compartments -- 2.4 Dynamics of Gene Gain and Gene Loss in Bacteria -- 2.5 ATP Regulation of Bacterial Replication -- 2.6 Redox Poise Across Bioenergetic Membranes -- 2.7 Allometric Scaling of Metabolic Rate and Complexity -- 2.8 Conclusions -- References -- 3 Origin, Function, and Transmission of Mitochondria -- 3.1 Introduction -- 3.2 Origins of Mitochondria -- 3.3 Mitochondrial Genomes -- 3.4 The Mitochondrial Theory of Ageing -- 3.5 Why Are There Genes in Mitochondria? -- 3.6 Co-location of Gene and Gene Product Permits Redox Regulation of Gene Expression -- 3.7 Maternal Inheritance of Mitochondria -- 3.8 Conclusions -- References -- 4 Mitochondria and Their Host: Morphology to Molecular Phylogeny -- 4.1 Introduction -- 4.2 Alternative Visions -- 4.3 Before the Word -- 4.4 Les Symbiotes -- 4.5 Symbionticism and the Origin of Species -- 4.6 Against the Current -- 4.7 Infective Heredity -- 4.8 The Tipping Point -- 4.9 The Birth of Bacterial Phylogenetics -- 4.10 Just-So Stories -- 4.11 Kingdom Come, Kingdom Go -- 4.12 A Chimeric Paradigm -- 4.13 Recapitulation -- References -- 5 Anaerobic Mitochondria: Properties and Origins -- 5.1 Introduction -- 5.2 Possible Variants in Anaerobic Metabolism -- 5.3 Cytosolic Adaptations to an Anaerobic Energy Metabolism -- 5.4 Anaerobically Functioning ATP-Generating Organelles -- 5.5 Energy Metabolism in Anaerobically Functioning Mitochondria -- 5.6 Adaptations in Electron-Transport Chains in Anaerobic Mitochondria -- 5.7 Structural Aspects of Anaerobically Functioning Electron- Transport Chains -- 5.8 Evolutionary Origin of Anaerobic Mitochondria -- 5.9 Conclusion -- References. , 6 Iron-Sulfur Proteins and Iron-Sulfur Cluster Assembly in Organisms with Hydrogenosomes and Mitosomes -- 6.1 Introduction -- 6.2 Mitochondrion-Related Organelles in "Amitochondriate" Eukaryotes -- 6.3 Iron-Sulfur Cluster, an Ancient Indispensable Prosthetic Group -- 6.4 Iron-Sulfur Proteins in Mitochondria and Other Cell Compartments -- 6.5 Iron-Sulfur Proteins in Organisms Harboring Hydrogenosomes and Mitosomes -- 6.6 Iron-Sulfur Cluster Assembly Machineries -- 6.7 Iron-Sulfur Cluster Biosynthesis and the Evolution of Mitochondria -- References -- 7 Hydrogenosomes (and Related Organelles, Either) Are Not the Same -- 7.1 Introduction -- 7.2 Hydrogenosomes and Mitochondrial-Remnant Organelles Evolved Repeatedly: Evidence from ADP/ATP Carriers -- 7.3 Functional Differences Between Mitochondrial and Alternative ADP/ATP Transporters -- 7.4 Evolutionary Tinkering in the Evolution of Hydrogenosomes -- 7.5 Why an [Fe]-Only Hydrogenase? -- 7.6 Conclusions -- References -- 8 The Chimaeric Origin of Mitochondria: Photosynthetic Cell Enslavement, Gene-Transfer Pressure, and Compartmentation Efficiency -- 8.1 Key Early Ideas -- 8.2 The Host Was a Protoeukaryote Not an Archaebacterium -- 8.3 Was the Slave Initially Photosynthetic? -- 8.4 Three Phases of α-proteobacterial Enslavement -- 8.5 Did Syntrophy or Endosymbiosis Precede Enslavement? -- 8.6 The Chimaeric Origin of Mitochondrial Protein Import and Targeting -- 8.7 Stage 2: Recovery from Massive Organelle-Host Gene Transfer -- 8.8 Mitochondrial Diversification -- 8.9 Conceptual Aspects of Megaevolution -- 8.10 Relative Genomic Contributions of the Two Partners -- 8.11 Genic Scale, Tempo, and Timing of Mitochondrial Enslavement and Eukaryote Origin -- References -- 9 Constantin Merezhkowsky and the Endokaryotic Hypothesis -- 9.1 Introduction -- 9.2 Modern Hypotheses of Eukaryotic Origin. , 9.3 Chimeric Nature of a Pro-eukaryote -- 9.4 Mitochondrial Origin and Eukaryogenesis -- 9.5 Conclusions -- References -- 10 The Diversity of Mitochondrion-Related Organelles Amongst Eukaryotic Microbes -- 10.1 Introduction -- 10.2 Diversity of Anaerobic Protists with Mitochondrion-Related Organelles -- 10.3 The Origins of Mitochondria, Mitosomes and Hydrogenosomes -- 10.4 Concluding Remarks -- References -- 11 Mitosomes of Parasitic Protozoa: Biology and Evolutionary Significance -- 11.1 Introduction -- 11.2 Discovery of Mitosomes: a Brief History -- 11.3 Mitosome Biology -- 11.4 Protein Import -- 11.5 Evolutionary Considerations -- 11.6 Conclusions -- References -- Index.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 47 (1998), S. 190-199 
    ISSN: 1432-1432
    Keywords: Key words: Amitochondriate protist — Glyceraldehyde-3-phosphate dehydrogenase — Glycolysis — Parabasala — Protein evolution —Trichomitus batrachorum— Trichomonadinae — Tritrichomonadinae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Over 90% of the open reading frame of gap genes for glycolytic glyceraldehyde-3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) was obtained with PCR from five species of Parabasala. With gap1 from Trichomonas vaginalis obtained earlier, the data include two sequences each for three species. All sequences were colinear with T. vaginalis gap1 and shared with it as a synapomorphy a 10- to 11-residue insertion not found in any other gap and an S-loop with characteristic features of eubacterial GAPDH. All residues known to be highly conserved in this enzyme were present. The parabasalid sequences formed a robust monophyletic group in phylogenetic reconstructions with distance-based, maximum-parsimony, and maximum-likelihood methods. The two genes of the amphibian commensal, Trichomitus batrachorum, shared a common ancestor with the rest, which separate into two well-supported lineages. T. vaginalis and Tetratrichomonas gallinarum (both representatives of Trichomonadinae) formed one, while Monocercomonas sp. and Tritrichomonas foetus formed the other. These data agreed with and/or were close to published reconstructions based on other macromolecules. They did not support the ancestral position of Monocercomonas sp. proposed on the basis of morphological characteristics but confirmed an early emergence of Trichomitus batrachorum. The sequence pairs obtained from three species indicated either gene duplications subsequent to the divergence of the corresponding lineages or a strong gene conversion later in these lineages. The parabasalid clade was a robust part of the eubacterial radiation of GAPDH and showed no relationships to the clade that contained all other eukaryotic gap genes. The data clearly reveal that the members of this lineage use in their glycolytic pathway a GAPDH species with properties and an evolutionary history that are unique among all eukaryotes studied so far.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1432
    Keywords: Hydrogenosome ; Molecular phylogeny ; Anaerobic protist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the eukaryotic unicellular organismTrichomonas vaginalis a key step of energy metabolism, the oxidative decarboxylation of pyruvate with the formation of acetyl-CoA, is catalyzed by the iron-sulfur protein pyruvate:ferredoxin oxidoreductase (PFO) and not by the almost-ubiquitous pyruvate dehydrogenase multienzyme complex. This enzyme is localized in the hydrogenosome, an organelle bounded by a double membrane. PFO and its closely related homolog, pyruvate: flavodoxin oxidoreductase, are enzymes found in a number of archaebacteria and eubacteria. The presence of these enzymes in eukaryotes is restricted, however, to a few amitochondriate groups. To gain more insight into the evolutionary relationships ofT. vaginalis PFO we determined the primary structure of its two genes (pfoA andpfoB). The deduced amino acid sequences showed 95% positional identity. Motifs implicated in related enzymes in liganding the Fe-S centers and thiamine pyrophosphate were well conserved. TheT. vaginalis PFOs were found to be homologous to eubacterial pyruvate: flavodoxin oxidoreductases and showed about 40% amino acid identity to these enzymes over their entire length. Lack of eubacterial PFO sequences precluded a comparison.pfoA andpfoB revealed a greater distance from related enzymes of Archaebacteria. The conceptual translation of the nucleotide sequences predicted an amino-terminal pentapeptide not present in the mature protein. This processed leader sequence was similar to but shorter than leader sequences noted in other hydrogenosomal proteins. These sequences are assumed to be involved in organellar targeting and import. The results underscore the unusual characteristics ofT. vaginalis metabolism and of their hydrogenosomes. They also suggest that in its energy metabolismT. vaginalis is closer to eubacteria than archaebacteria.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-1432
    Keywords: Hydrogenosome ; Molecular phylogeny ; Anaerobic protist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the eukaryotic unicellular organism Trichomonas vaginalis a key step of energy metabolism, the oxidative decarboxylation of pyruvate with the formation of acetyl-CoA, is catalyzed by the iron-sulfur protein pyruvate:ferredoxin oxidoreductase (PFO) and not by the almost-ubiquitous pyruvate dehydrogenase multienzyme complex. This enzyme is localized in the hydrogenosome, an organelle bounded by a double membrane. PFO and its closely related homolog, pyruvate: flavodoxin oxidoreductase, are enzymes found in a number of archaebacteria and eubacteria. The presence of these enzymes in eukaryotes is restricted, however, to a few amitochondriate groups. To gain more insight into the evolutionary relationships of T. vaginalis PFO we determined the primary structure of its two genes (pfoA and pfoB). The deduced amino acid sequences showed 95% positional identity. Motifs implicated in related enzymes in liganding the Fe-S centers and thiamine pyrophosphate were well conserved. The T. vaginalis PFOs were found to be homologous to eubacterial pyruvate: flavodoxin oxidoreductases and showed about 40% amino acid identity to these enzymes over their entire length. Lack of eubacterial PFO sequences precluded a comparison. pfoA and pfoB revealed a greater distance from related enzymes of Archaebacteria. The conceptual translation of the nucleotide sequences predicted an amino-terminal pentapeptide not present in the mature protein. This processed leader sequence was similar to but shorter than leader sequences noted in other hydrogenosomal proteins. These sequences are assumed to be involved in organellar targeting and import. The results underscore the unusual characteristics of T. vaginalis metabolism and of their hydrogenosomes. They also suggest that in its energy metabolism T. vaginalis is closer to eubacteria than archaebacteria.
    Type of Medium: Electronic Resource
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  • 5
    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
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  • 6
    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
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  • 7
    ISSN: 1432-1432
    Keywords: Glyceraldehyde-3-phosphate dehydrogenase ; Amitochondriate protist ; Protein evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), localized in the cytosol of Trichomonas vaginalis, was partially purified. The enzyme is specific for NAD+ and is similar in most of its catalytic properties to glycolytic GAPDHs from other organisms. Its sensitivity to koningic acid is similar to levels observed in GAPDHs from eubacteria and two orders of magnitude lower than those observed for eukaryotic GAPDHs. The complete amino acid sequence of T. vaginalis GAPDH was derived from the N-terminal sequence of the purified protein and the deduced sequence of a cDNA clone. It showed great similarity to other eubacterial and eukaryotic GAPDH sequences. The sequence of the S-loop displayed a eubacterial signature. The overall sequence was more similar to eubacterial sequences than to cytosolic and glycosomal eukaryotic sequences. In phylogenetic trees obtained with distance matrix and parsimony methods T. vaginalis GAPDH clustered with its eubacterial homologs. GAPDHs of other amitochondriate protists, belonging to early branches of the eukaryotic lineage (Giardia lamblia and Entamoeba histolytica—Smith M.W. and Doolittle R.F., unpublished data in GenBank), showed typical eukaryotic signatures and clustered with other eukaryotic sequences, indicating that T. vaginalis GAPDH occupies an anomalous position, possibly due to horizontal gene transfer from a eubacterium.
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 135 (1996), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The nucleotide sequence of a gene coding for a 37 kDa subunit of a cytosolic malate dehydrogenase of Trichomonas vaginalis was established. The sequences of a gDNA clone and a cDNA clone, which lacked seven amino-terminal codons, were identical, indicating an absence of introns from the gene. Cell fractionation combined with sequencing of peptide fragments of the purified enzyme showed that the gene codes for an expressed cytosolic enzyme. The derived amino acid sequence was closely related to cytosolic malate dehydrogenases from animals and plants and from the eubacteria Thermus aquaticus and Mycobacterium leprae and was more distant from the enzyme of mitochondria and from Escherichia coli and certain other eubacteria. In phylogenetic reconstructions this enzyme shared a most recent common ancestor with other cytosolic enzymes.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 110 (1993), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The parasitic protist Trichomonas vaginalis transport glucose across the plasma membrane by facilitated diffusion. The Km of the transporter for glucose was 1.6 mM. The uptake of labelled glucose in a minimal medium not allowing growth reached saturation only after 2.5 h, indicating the turnover of storage carbohydrate. Organisms grown on glucose showed higher activities both of the transporter and of the subsequent metabolic pathway than organisms grown on maltose. At low external glucose concentrations the transport step was rate limiting, at higher levels a subsequent enzymatic step. The uptake mechanism for glucose of T. vaginalis resembled that of parasitic kinetoplastid protist and Entamoeba histolytica.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 187 (1960), S. 65-65 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Cells of T. corlissi, grown axenically on a tryptone (1 per cent) and yeast extract (0-05 per cent) broth, were washed twice in Prescott solution and kept during the experiments in the same solution. Fresh frozen sections of rat spleen served as food. The animals readily ingested the spleen cells. ...
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