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Bio Systems 1985Zoospores of Oomycetes contain a variety of microbody-like organelles with highly structured matrices. Although in general their function is unknown, the appearance of... (Review)
Review
Zoospores of Oomycetes contain a variety of microbody-like organelles with highly structured matrices. Although in general their function is unknown, the appearance of similar organelles in related taxa suggests the ultrastructural differences could be used as taxonomic characters. This study surveys microbody-like organelles of oomycetous zoospores to determine if this is an additional criterion by which the phylogeny of these fungi can be evaluated. In zoospores of the order Saprolegniales, kinetosome-associated organelles (K-bodies) are found which typically consist of tubular and/or granular matrices. K-bodies are not found associated with kinetosomes in zoospores of the Peronosporales, but microbodies containing tubules, and in some genera marginal plates, are located near the kinetosomes, along the groove, and in other peripheral areas. K-bodies have been reported in only one member of the order Lagenidiales. These K-bodies lack a granular matrix, but contain a single curved plate from which tubules arise, forming a cone. In the one genus of the Leptomitales examined, a similar K-body contains a plate and scattered tubules. Organisms with similar microbody-like organelles are probably more closely related than those with different types of microbody-like organelles. The presence of an organelle resembling K-bodies in zoospores of an alga in the Tribophyceae supports the phylogenetic association between algae and Oomycetes. A complete survey of Oomycete genera may well reveal intermediates between the structurally different types of microbody-like organelles, allowing the reconstruction of the phylogenetic history of an organelle.
Topics: Biological Evolution; Chytridiomycota; Eukaryota; Microbodies; Microscopy, Electron; Oomycetes; Organoids; Phylogeny
PubMed: 3910137
DOI: 10.1016/0303-2647(85)90032-2 -
Experimental Parasitology Oct 1989
Review
Topics: Animals; Glycolysis; Microbodies; Trypanosoma brucei brucei
PubMed: 2676581
DOI: 10.1016/0014-4894(89)90079-9 -
The Journal of Histochemistry and... Nov 1973
Review
Topics: Cholesterol; Clofibrate; Hydrogen Peroxide; Microbodies; Nafenopin; Organoids; Propionates; Steroids
PubMed: 4587529
DOI: 10.1177/21.11.967 -
Tanpakushitsu Kakusan Koso. Protein,... Jul 1987
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Biochemical Society Transactions Feb 2021Kinetoplastid parasites have essential organelles called glycosomes that are analogous to peroxisomes present in other eukaryotes. While many of the processes that... (Review)
Review
Kinetoplastid parasites have essential organelles called glycosomes that are analogous to peroxisomes present in other eukaryotes. While many of the processes that regulate glycosomes are conserved, there are several unique aspects of their biology that are divergent from other systems and may be leveraged as therapeutic targets for the treatment of kinetoplastid diseases. Glycosomes are heterogeneous organelles that likely exist as sub-populations with different protein composition and function in a given cell, between individual cells, and between species. However, the limitations posed by the small size of these organelles makes the study of this heterogeneity difficult. Recent advances in the analysis of small vesicles by flow-cytometry provide an opportunity to overcome these limitations. In this review, we describe studies that document the diverse nature of glycosomes and propose an approach to using flow cytometry and organelle sorting to study the diverse composition and function of these organelles. Because the cellular machinery that regulates glycosome protein import and biogenesis is likely to contribute, at least in part, to glycosome heterogeneity we highlight some ways in which the glycosome protein import machinery differs from that of peroxisomes in other eukaryotes.
Topics: Animals; Kinetoplastida; Microbodies; Peroxisomes; Protein Transport; Protozoan Proteins
PubMed: 33439256
DOI: 10.1042/BST20190517 -
Current Opinion in Cell Biology Aug 1989
Review
Topics: Adenosine Triphosphatases; Amino Acid Sequence; Animals; Biological Transport, Active; Intracellular Membranes; Microbodies; Models, Biological; Molecular Sequence Data; Mutation; Proteins
PubMed: 2534044
DOI: 10.1016/0955-0674(89)90026-4 -
Functional & Integrative Genomics May 2009In the filamentous fungus Penicillium chrysogenum, microbodies are essential for penicillin biosynthesis. To better understand the role of these organelles in...
In the filamentous fungus Penicillium chrysogenum, microbodies are essential for penicillin biosynthesis. To better understand the role of these organelles in antibiotics production, we determined the matrix enzyme contents of P. chrysogenum microbodies. Using a novel in silico approach, we first obtained a catalogue of 200 P. chrysogenum proteins with putative microbody targeting signals (PTSs). This included two orthologs of proteins involved in cephalosporin biosynthesis, which we demonstrate to be bona fide microbody matrix constituents. Subsequently, we performed a proteomics based inventory of P. chrysogenum microbody matrix proteins using nano-LC-MS/MS analysis. We identified 89 microbody proteins, 79 with a PTS, including the two known microbody-borne penicillin biosynthesis enzymes, isopenicillin N:acyl CoA acyltransferase and phenylacetyl-CoA ligase. Comparative analysis revealed that 69 out of 79 PTS proteins identified experimentally were in the reference list. A prominent microbody protein was identified as a novel fumarate reductase-cytochrome b5 fusion protein, which contains an internal PTS2 between the two functional domains. We show that this protein indeed localizes to P. chrysogenum microbodies.
Topics: Amino Acid Sequence; Base Sequence; DNA Primers; DNA, Fungal; Fungal Proteins; Genome, Fungal; Microbodies; Microscopy, Electron, Transmission; Molecular Sequence Data; Penicillins; Penicillium chrysogenum; Plasmids; Protein Sorting Signals; Proteome; Proteomics; Recombinant Proteins; Tandem Mass Spectrometry
PubMed: 19156454
DOI: 10.1007/s10142-009-0110-6 -
Biochemical Genetics Apr 1978
Review
Topics: Alcohol Oxidoreductases; Animals; Catalase; D-Amino-Acid Oxidase; Genes; Hydroxy Acids; Malate Dehydrogenase; Mice; Microbodies; Mutation; Organoids; Plants; Urate Oxidase
PubMed: 28117
DOI: 10.1007/BF00484076 -
Annual Review of Cell Biology 1985
Review
Topics: Animals; Catalase; Cell Compartmentation; Child, Preschool; DNA; Endoplasmic Reticulum; Glycoproteins; Humans; Membrane Proteins; Metabolism, Inborn Errors; Microbodies; Morphogenesis; Oxidoreductases
PubMed: 3916321
DOI: 10.1146/annurev.cb.01.110185.002421 -
Neurochemical Research Apr 1999The enzymes involved in beta-oxidation spiral are schematically classified into two groups. The first group consists of palmitoyl-CoA oxidase, the L-bifunctional... (Review)
Review
The enzymes involved in beta-oxidation spiral are schematically classified into two groups. The first group consists of palmitoyl-CoA oxidase, the L-bifunctional protein, which has been called as the bifunctional protein, and 3-ketoacyl-CoA thiolase. The second group consists of the newly confirmed enzymes, branched chain oxidase, the D-bifunctional protein, and sterol carrier protein x. The enzymes of the first group are inducible and act on the straight chain acyl-CoA substrates. But the enzymes of the second group are non-inducible and act on branched chain acyl-CoAs. Accordingly, bile acid formation and oxidation of pristanic acid derived from phytol are catalyzed by the enzymes of the second group but not by those of the first group. The functions of the peroxisomal system and methods of analysis of the enzymes are briefly summarized.
Topics: Animals; Enzymes; Fatty Acids; Humans; Microbodies; Mitochondria; Oxidation-Reduction
PubMed: 10227687
DOI: 10.1023/a:1022540030918