-
Biochemical Society Transactions Feb 1990
Review
Topics: Amino Acids; Animals; Humans; Lipid Metabolism; Microbodies; Purines
PubMed: 2185099
DOI: 10.1042/bst0180087 -
Advances in Microbial Physiology 1983
Review
Topics: Alcohol Oxidoreductases; Catalase; Formaldehyde; Fungal Proteins; Methanol; Methylamines; Microbodies; Spores, Fungal; Yeasts
PubMed: 6364725
DOI: 10.1016/s0065-2911(08)60384-7 -
Annals of the New York Academy of... Dec 1996
Topics: Animals; CHO Cells; Cricetinae; Microbodies; Microtubules; Motion
PubMed: 8993587
DOI: 10.1111/j.1749-6632.1996.tb18659.x -
Annals of the New York Academy of... 1982
Review
Topics: Allylisopropylacetamide; Animals; Carnitine O-Acetyltransferase; Catalase; Clofibrate; Kidney; Lipid Metabolism; Lipofuscin; Liver; Mice; Microbodies; Mitotane; Organoids; Peptides; Phenobarbital; Rats
PubMed: 7046570
DOI: 10.1111/j.1749-6632.1982.tb21409.x -
Trends in Biochemical Sciences Jul 1988
Review
Topics: Amino Acid Sequence; Animals; Eukaryota; Microbodies; Molecular Sequence Data; Trypanosoma
PubMed: 3076722
DOI: 10.1016/0968-0004(88)90158-2 -
Mechanisms of Ageing and Development May 1995This article reviews the available data on the role of the peroxisome in the growth, differentiation and degeneration of mammalian tissues. Developmental progressions of... (Review)
Review
This article reviews the available data on the role of the peroxisome in the growth, differentiation and degeneration of mammalian tissues. Developmental progressions of peroxisomes are described, along with the influence of inhibitors of peroxisomal enzymes, peroxisome proliferators and morphogenetic agents on the ontogeny of experimental animals. The role of the peroxisome in protecting tissues from damage by oxygen free radicals is also described, as is the changing role of the peroxisome in the ageing animal. Amongst the degenerative diseases which have been associated with free radical damage are cancer, atherosclerosis, muscular dystrophy, rheumatoid arthritis and the senile degeneration of brain function. In all these conditions, the major characteristics of molecular damage have been considered, along with the particular role of the peroxisome in alleviating these effects. Proposals for further research into peroxisomal function during ontogeny and the degenerative changes associated with ageing are developed, and the possibility of palliative treatments discussed.
Topics: Aging; Animals; Cell Differentiation; Free Radicals; Microbodies; Nerve Degeneration
PubMed: 7564565
DOI: 10.1016/0047-6374(94)01563-2 -
Critical Reviews in Biotechnology 1996Among aroma compounds interesting for the food industry, lactones may be produced by biotechnological means using yeasts. These microorganisms are able to synthesize... (Review)
Review
Among aroma compounds interesting for the food industry, lactones may be produced by biotechnological means using yeasts. These microorganisms are able to synthesize lactones de novo or by biotransformation of fatty acids with higher yields. Obtained lactone concentrations are compatible with industrial production, although detailed metabolic pathways have not been completely elucidated. The biotransformation of ricinoleic acid into gamma-decalactone is taken here as an example to better understand the uptake of hydroxy fatty acids by yeasts and the different pathways of fatty acid degradation. The localization of ricinoleic acid beta-oxidation in peroxisomes is demonstrated. Then the regulation of the biotransformation is described, particularly the induction of peroxisome proliferation and peroxisomal beta-oxidation and its regulation at the genome level. The nature of the biotransformation product is then discussed (4-hydroxydecanoic acid or gamma-decalactone), because the localization and the mechanisms of the lactonization are still not properly known. Lactone production may also be limited by the degradation of this aroma compound by the yeasts which produced it. Thus, different possible ways of modification and degradation of gamma-decalactone are described.
Topics: Biotransformation; Cell Division; Culture Media; Fungi; Lactones; Microbodies; Oxidation-Reduction; Ricinoleic Acids; Yeasts
PubMed: 8989867
DOI: 10.3109/07388559609147424 -
Biological Chemistry Feb 2023Oxalyl-CoA synthetase from is one of the most abundant peroxisomal proteins in yeast and hence has become a model to study peroxisomal translocation. It contains a...
Oxalyl-CoA synthetase from is one of the most abundant peroxisomal proteins in yeast and hence has become a model to study peroxisomal translocation. It contains a C-terminal Peroxisome Targeting Signal 1, which however is partly dispensable, suggesting additional receptor bindings sites. To unravel any additional features that may contribute to its capacity to be recognized as peroxisomal target, we determined its assembly and overall architecture by an integrated structural biology approach, including X-ray crystallography, single particle cryo-electron microscopy and small angle X-ray scattering. Surprisingly, it assembles into mixture of concentration-dependent dimers, tetramers and hexamers by dimer self-association. Hexameric particles form an unprecedented asymmetric horseshoe-like arrangement, which considerably differs from symmetric hexameric assembly found in many other protein structures. A single mutation within the self-association interface is sufficient to abolish any higher-level oligomerization, resulting in a homogenous dimeric assembly. The small C-terminal domain of yeast Oxalyl-CoA synthetase is connected by a partly flexible hinge with the large N-terminal domain, which provides the sole basis for oligomeric assembly. Our data provide a basis to mechanistically study peroxisomal translocation of this target.
Topics: Saccharomyces cerevisiae; Amino Acid Sequence; Cryoelectron Microscopy; Microbodies; Saccharomyces cerevisiae Proteins; Ligases
PubMed: 36694962
DOI: 10.1515/hsz-2022-0273 -
Bio Systems Apr 1978Chytridiomycetous fungal zoospores contain a unique and intricate association of organelles, the 'microbody-lipid globule complex' (MLC). The spatial arrangement of... (Comparative Study)
Comparative Study
Chytridiomycetous fungal zoospores contain a unique and intricate association of organelles, the 'microbody-lipid globule complex' (MLC). The spatial arrangement of organelles in the MLC appears important in the utilization of lipid globules for energy, but in addition, the structural association of organelles in the MLC reveals phylogenetic trends within this diverse group of organisms. Variations in the structure of the MLC correlate well with current phylogenetic concepts of aquatic fungi, yet suggest new relationships among these posteriorly uniflagellate zoospores. Based upon the organization of organelles in the MLC, 4 basic patterns of MLCs can be recognized, and these correspond to the 4 orders of Chytridiomycetes. The MLC in its simplest form consists of a microbody appressed to the edge of a lipid globule. In more highly organized MLCs, mitochondria subtend the microbody and a cisterna surmounts one side of the lipid globule. The organization and structure is still more complex in other MLCs where ER is elaborated into a tubular network of membranes or where small microbodies or mitochondria fuse into 'giant' organelles. The structural organization of the MLC provides an additional criterion by which the phylogeny of awuatic fungi can be evaluated.
Topics: Fungi; Lipids; Microbodies; Organoids; Phylogeny; Species Specificity; Spores, Fungal
PubMed: 656565
DOI: 10.1016/0303-2647(78)90038-2 -
The EMBO Journal Jun 1986To determine how microbody enzymes enter microbodies, we are studying the genes for glycosomal (microbody) enzymes in Trypanosoma brucei. Here we present our results for... (Comparative Study)
Comparative Study
To determine how microbody enzymes enter microbodies, we are studying the genes for glycosomal (microbody) enzymes in Trypanosoma brucei. Here we present our results for triosephosphate isomerase (TIM), which is found exclusively in the glycosome. We found a single TIM gene without introns, having one major polyadenylated transcript of 1500 nucleotides with a long untranslated tail of approximately 600 nucleotides. By a novel method, suitable for low abundance transcripts, we demonstrate that TIM mRNA contains the 35-nucleotide leader sequence (mini-exon) also found on several other trypanosome mRNAs. The TIM gene and a DNA segment of at least 6 kbp upstream of the gene are transcribed at an equal rate in isolated nuclei, suggesting that the gene is part of a much larger transcription unit. The predicted protein is of the same size as TIMs from other organisms and shares approximately 50% amino acid homology with other eukaryote TIMs, somewhat less with prokaryote TIMs. Trypanosome TIM is the most basic of all TIMs sequenced thus far. This is, in part, due to the presence of two clusters of positively charged residues in the molecule which may act as a signal for entry into glycosomes.
Topics: Amino Acid Sequence; Animals; Base Sequence; Carbohydrate Epimerases; DNA Restriction Enzymes; Genes; Humans; Microbodies; Sequence Homology, Nucleic Acid; Species Specificity; Triose-Phosphate Isomerase; Trypanosoma brucei brucei
PubMed: 3015595
DOI: 10.1002/j.1460-2075.1986.tb04358.x