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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
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 42 (1995), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . The complete nucleotide sequence has been established for two genes (maeA and maeB) coding for different subunits of the hydrogenosomal malic enzyme [malate dehydrogenase (decarboxylating) EC 1.1.1.39] of Trichomonas vaginalis. Two further genes (maeC and maeD) of this enzyme have been partially sequenced. The complete open reading frames code for polypeptides of 567 amino acids in length. These two open reading frames are similar with less than 12 percent pairwise nucleotide differences and less than 9 percent pairwise amino acid differences. The open reading frames of the two partially sequenced genes correspond to the amino-terminal part of the polypeptides coded and are similar to the corresponding parts of the completely sequenced ones. The deduced translation products of the two complete genes differ in their calculated pI values by 1.5 pH unit. The genes code for polypeptides which contain 12 or 11 amino-terminal amino-acyl residues not present in the proteins isolated from the cell. Other hydrogenosomal enzymes also have similar amino-terminal extensions which probably play a role in organellar targeting and translocation of the newly synthesized polypeptides. A comparison of 19 related enzymes from bacteria and eukaryotes with the maeA product revealed 34–45 percent amino acid identity. Phylogenetic reconstruction based on nonconservative amino acid differences with maximum parsimony (phylogenetic analysis using parsimony, PAUP) and distance based (neighbor-joining, NJ) methods showed that the T. vaginalis enzyme is the most divergent of all eukaryotic malic enzymes, indicating its long independent evolutionary history.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Complete nucleotide sequences have been established for two genes (gap1 and gap2) coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) homologs in the diplomonad Giardia lamblia. In addition, almost complete sequences of the GAPDH open reading frames were obtained from PCR products for two free-living diplomonad species, Trepomonas agilis and Hexamita inflata, and a parasite of Atlantic salmon, an as yet unnamed species with morphological affinities to Spironucleus. Giardia lamblia gap 1 and the genes from the three other diplomonad species show high similarity to each other and to other glycolytic GAPDH genes. All amino-acyl residues known to be highly conserved in this enzyme are also conserved in these sequences. Giardia lamblia gap2 gene is more divergent and its putative translation reveals the presence of a cysteine and serine-rich insertion resembling a metal binding finger. This motif has not yet been noted in other GAPDH molecules. All sequences contain an S-loop signature with characteristics close to those of eukaryotes. In phylogenetic reconstructions based on the derived amino acid sequences with neighborjoining, parsimony and maximum-likelihood methods the four typical GAPDH sequences of diplomonads cluster into a single clade. Within this clade, G. lamblia gap1 shares a common ancestor with the rest of the genes. The latter are more closely related to each other, indicating an early separation of the lineage leading to the genus Giardia from the lineage encompassing the morphologically less differentiated genera, Trepomonas, Hexamita and that of the unnamed species. This result is discordant with the orthogonal evolution of diplomonads suggested on the basis of comparative morphology. In neighbor-joining reconstructions G. lamblia gap2 occupies a variable position, due to its great divergence. In parsimony and maximum likelihood analysis however, it shares a most recent common ancestor with the typical G. lamblia gap1 gene, suggesting that it diverged after the separation of the Giardia lineage. The position of the diplomonad clade in broader phylogenetic reconstructions is firmly within the typical cytosolic glycolytic representatives of GAPDH of eukaryotes.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Small subunit (16S-like) ribosomal RNA sequences were obtained from representatives of all four families constituting the order Trichomonadida. Comparative sequence analysis revealed that the Trichomonadida are a monophyletic lineage and a deep branch of the eukaryotic tree. Relative to other early divergent eukaryotic assemblages the branching pattern within the Trichomonadida is very shallow. This pattern suggests the Trichomonadida radiated recently, perhaps in conjunction with their animal hosts. From a morphological perspective the Devescovinidae and Calonymphidae are considered more derived than the Monocercomonadidae and Trichomonadidae. Molecular trees inferred by distance, parsimony and likelihood techniques consistently show the Devescovinidae and Calonymphidae are the earliest diverging lineages within the Trichomonadida, however bootstrap values do not strongly support a particular branching order. In an analysis of all known 16S-like ribosomal RNA sequences, the Trichomonadida share most recent common ancestry with unidentified protists from the hindgut of the termite Reticulitermes flavipes. The position of two putative free-living trichomonads in the tree is indicative of derivation from symbionts rather than direct descent from some free-living ancestral trichomonad.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 32 (1985), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 168 (1969), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . The taxonomic position and phylogenetic relationships of the Pelobionta, an amitochondriate amoeboflagellate group, are not yet completely settled. To provide more information, we obtained sequences for the large subunit rDNA gene, the gene for translation elongation factor la, and for a large part of the gene encoding translation elongation factor 2 from a representative of this group. Mastigamoeba balamuthi (formerly Phreatamoeba balamuthi). The gene for the large subunit rDNA was unusually large compared to those of other protists, a phenomenon that had previously been observed for the gene encoding the small subunit rDNA. Phylogenetic reconstruction using a maximum likelihood method was performed with these sequences, as well as the gene encoding the small subunit rDNA. When evaluated individually, the M. balamuthi genes for the small and large subunit rDNAs and elongation factor 1α had a most recent common ancestor with either the Mycetozoa (slime molds) or with Entamoeba histolytica. A clade formed by M. balamuthi, E. histolytica, and Mycetozoa was not rejected statistically for any of the sequences. A combined maximum likelihood analysis using 3,935 positions from all molecules suggested that these three taxonomic units form a robust clade. We were unable to resolve the closest group to this clade using the combined analysis. These findings support the notion, which had previously been proposed primarily on cytological evidence, that both M. balamuthi and E. histolytica are closely related to the Mycetozoa and that these three together represent a major eukaryotic lineage.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 47 (2000), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Two isoforms of α-glucosidase were purified from the parasitic protist Trichomonas vaginalia. Both consisted of 103 kDa subunits, but differed in pH optimum and substrate specificity. Isoform 1 had a pH optimum around 4.5 and negligible activity on glucose oligomcrs other than maltose, while isoform 2 with a pH optimum of 5.5 hydrolyzed also such substrates at considerable rates. Neither had activity on glycogen or starch. Isoform 1 had a specific activity for hydrolysis of maltose of 30 U/mg protein and isoform 2 101 U/mg protein. The Km values were 0.4 mM and 2.0 mM, respectively. Isoform 2 probably corresponds to the activity detected on the cell surface.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 21 (1974), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A primitive trichomonad, Monocercomonas sp. (strain NS-1:PRR) from Natrix sipedon, was grown axenically in Diamond's medium. Activity of NADH oxidase, malate dehydrogenase, malate dehydrogenase (decarboxylating) and of the anaerobic enzymes, pyruvate synthase and hydrogenase as well as of several hydrolases was demonstrated in homogenates. The subcellular distribution of these activities was studied by means of analytical differential and isopycnic centrifugation of homogenates prepared in 0.25 M sucrose. NADH oxidase and malate dehydrogenase are in the nonsedimentable part of the cytoplasm. Malate dehydrogenase (decarboxylating), pyruvate synthase, and hydrogenase are associated with a large particle which equilibrates at density 1.22. In its properties, this particle corresponds to the microbody-like hydrogenosomes of Tritrichomonas foetus. The 5 hydrolases studied are associated with at least 2 different particle populations: a large particle population equilibrating at densities from 1.10 to 1.16 is the exclusive location of 3 enzymes (β-galactosidase, protease and β-N-acetylglucosaminidase), 2 of which have a pH optimum close to neutrality. These particles contain part of the acid phosphatase and β-glucuronidase. Another part of these 2 enzymes is associated with a separate population of smaller granules with equilibrium densities of 1.16 to 1.18. The 2 types of hydrolase-carrying particles are also biochemically very similar to their counterparts in T. foetus.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 16 (1969), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: SYNOPSIS. Homogenates of axenic Acanthamoeba sp. had ribonuclease, phosphatase, proteinase, α-glucosidase, β-N-acetylglucosaminidase, and β-glucuronidase activities; all had acid pH optima. After isopycnic density-gradient centrifugation all showed the same relatively broad and unimodal distribution pattern, with a peak at a density of 1.17. This differs from the distribution of mitochondrial malate dehydrogenase and of peroxisomal urate oxidase and catalase. The findings are believed to reflect the occurrence of lysosomes in Acanthamoeba.
    Type of Medium: Electronic Resource
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