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Archives of Microbiology Nov 1996Aspergillus nidulans is able to grow on oleic acid as sole carbon source. Characterization of the oleate-induced beta-oxidation pathway showed the presence of the two...
Aspergillus nidulans is able to grow on oleic acid as sole carbon source. Characterization of the oleate-induced beta-oxidation pathway showed the presence of the two enzyme activities involved in the first step of this catabolic system: acyl-CoA oxidase and acyl-CoA dehydrogenase. After isopicnic centrifugation in a linear sucrose gradient, microbodies (peroxisomes) housing the beta-oxidation enzymes, isocitrate lyase and catalase were clearly resolved from the mitochondrial fraction, which contained fumarase. Growth on oleic acid was associated with the development of many microbodies that were scattered throughout the cytoplasm of the cells. These microbodies (peroxisomes) were round to elongated, made up 6% of the cytoplasmic volume, and were characterized by the presence of catalase. The beta-oxidation pathway was also induced in acetate-grown cells, although at lower levels; these cells lacked acyl-CoA oxidase activity. Nevertheless, growth on acetate did not cause a massive proliferation of microbodies in A. nidulans.
Topics: Acetates; Acetyl-CoA C-Acetyltransferase; Acyl-CoA Dehydrogenase; Acyl-CoA Dehydrogenases; Aspergillus nidulans; Catalase; Culture Media; Enoyl-CoA Hydratase; Fatty Acids; Fumarate Hydratase; Glucose; Isocitrate Lyase; Microbodies; Microscopy, Electron; Oleic Acid; Oxidation-Reduction
PubMed: 8929280
DOI: 10.1007/s002030050392 -
Virchows Archiv. B, Cell Pathology 1973
Topics: Animals; Clofibrate; Endoplasmic Reticulum; Hypophysectomy; Liver; Liver Neoplasms; Male; Microbodies; Microscopy, Electron; Microtubules; Organoids; Rats
PubMed: 4201012
DOI: 10.1007/BF02889178 -
The EMBO Journal Apr 1988To determine how microbody proteins enter microbodies, we have previously compared the genes for the cytosolic and glycosomal (microbody) phosphoglycerate kinases (PGKs)... (Comparative Study)
Comparative Study
To determine how microbody proteins enter microbodies, we have previously compared the genes for the cytosolic and glycosomal (microbody) phosphoglycerate kinases (PGKs) of Trypanosoma brucei and found the microbody enzyme to differ from other PGKs and the cytosolic form in two respects: a high net positive charge and a C-terminal extension of 20 amino acids (Osinga et al., 1985). Here we present the comparison of the genes for the cytosolic and glycosomal PGKs of Crithidia fasciculata, another kinetoplastid organism. The amino acid sequences of the two Crithidia isoenzymes are virtually identical, except for a C-terminal extension of 38 amino acids. We conclude that this extension must direct the glycosomal PGK to the glycosome. The extensions of the Crithidia and Trypanosoma enzymes are both rich in small hydrophobic and hydroxyl amino acids.
Topics: Amino Acid Sequence; Animals; Base Sequence; Crithidia; Cytosol; DNA; Genes; Genetic Linkage; Microbodies; Molecular Sequence Data; Phosphoglycerate Kinase; Sequence Homology, Nucleic Acid; Trypanosoma brucei brucei
PubMed: 3402434
DOI: 10.1002/j.1460-2075.1988.tb02926.x -
Cell Biochemistry and Function Sep 1992
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Journal of Proteomics Mar 2017Transport of penicillin intermediates and penicillin secretion are still poorly characterized in Penicillium chrysogenum (re-identified as Penicillium rubens). Calcium...
UNLABELLED
Transport of penicillin intermediates and penicillin secretion are still poorly characterized in Penicillium chrysogenum (re-identified as Penicillium rubens). Calcium (Ca) plays an important role in the metabolism of filamentous fungi, and casein phosphopeptides (CPP) are involved in Ca internalization. In this study we observe that the effect of CaCl and CPP is additive and promotes an increase in penicillin production of up to 10-12 fold. Combination of CaCl and CPP greatly promotes expression of the three penicillin biosynthetic genes. Comparative proteomic analysis by 2D-DIGE, identified 39 proteins differentially represented in P. chrysogenum Wisconsin 54-1255 after CPP/CaCl addition. The most interesting group of overrepresented proteins were a peroxisomal catalase, three proteins of the methylcitrate cycle, two aminotransferases and cystationine β-synthase, which are directly or indirectly related to the formation of penicillin amino acid precursors. Importantly, two of the enzymes of the penicillin pathway (isopenicillin N synthase and isopenicillin N acyltransferase) are clearly induced after CPP/CaCl addition. Most of these overrepresented proteins are either authentic peroxisomal proteins or microbody-associated proteins. This evidence suggests that addition of CPP/CaCl promotes the formation of penicillin precursors and the penicillin biosynthetic enzymes in peroxisomes and vesicles, which may be involved in transport and secretion of penicillin.
SIGNIFICANCE
Penicillin biosynthesis in Penicillium chrysogenum is one of the best characterized secondary metabolism processes. However, the mechanism by which penicillin is secreted still remains to be elucidated. Taking into account the role played by Ca and CPP in the secretory pathway and considering the positive effect that Ca exerts on penicillin production, the analysis of global protein changes produced after CPP/CaCl addition is very helpful to decipher the processes related to the biosynthesis and secretion of penicillin.
Topics: Calcium Chloride; Caseins; Fungal Proteins; Microbodies; Penicillins; Penicillium chrysogenum; Peroxisomes; Phosphopeptides
PubMed: 28062375
DOI: 10.1016/j.jprot.2016.12.021 -
FEBS Letters Jun 1978
Topics: Candida; Cell Nucleus; Centrifugation, Isopycnic; DNA; DNA, Mitochondrial; Microbodies; Organoids
PubMed: 668895
DOI: 10.1016/0014-5793(78)80393-7 -
Physiological Reviews Jan 1998In the decade that has elapsed since the discovery of the first peroxisomal targeting signal (PTS), considerable information has been obtained regarding the mechanism of... (Review)
Review
In the decade that has elapsed since the discovery of the first peroxisomal targeting signal (PTS), considerable information has been obtained regarding the mechanism of protein import into peroxisomes. The PTSs responsible for the import of matrix and membrane proteins to peroxisomes, the receptors for several of these PTSs, and docking proteins for the PTS1 and PTS2 receptors are known. Many peroxins involved in peroxisomal protein import and biogenesis have been characterized genetically and biochemically. These studies have revealed important new insights regarding the mechanism of protein translocation across the peroxisomal membrane, the conservation of PEX genes through evolution, the role of peroxins in fatal human peroxisomal disorders, and the biogenesis of the organelle. It is clear that peroxisomal protein import and biogenesis have many features unique to this organelle alone. More recent studies on peroxisome degradation, division, and movement highlight newer aspects of the biology of this organelle that promise to be just as exciting and interesting as import and biogenesis.
Topics: Animals; Humans; Membrane Proteins; Microbodies; PHEX Phosphate Regulating Neutral Endopeptidase; Peroxisomal Disorders; Protein Biosynthesis; Protein Conformation; Proteins; Signal Transduction
PubMed: 9457172
DOI: 10.1152/physrev.1998.78.1.171 -
AJNR. American Journal of Neuroradiology 1991
Topics: Biopsy; Child; Humans; Liver; Microbodies; Phytanic Acid; Refsum Disease
PubMed: 1722385
DOI: No ID Found -
Annals of the New York Academy of... 1982
Topics: Microbodies; Organoids
PubMed: 6953841
DOI: No ID Found -
Microscopy Research and Technique May 1995Peroxisomes, since their discovery as microbodies, have been studied mostly independently by electron microscopists and biochemists. The fine structure has been studied... (Review)
Review
Peroxisomes, since their discovery as microbodies, have been studied mostly independently by electron microscopists and biochemists. The fine structure has been studied by electron microscopy, and the compositional enzymes and proteins by protein biochemistry. Electron microscopic histochemistry has been used to try to clarify the relationship between the fine structure and its constituents. The immunogold technique, a combination of electron microscopy and protein biochemistry, for the first time resolved this problem due to the high sensitivity and resolution power of the staining and the high reliability of the technique. The present paper reviews the way in which the immunogold techniques, especially the protein A-gold technique, revealed the localization of various enzymes or proteins in peroxisomes or peroxisomal subcompartments, and discusses why this technique should be employed in peroxisome research.
Topics: Animals; Enzymes; Immunohistochemistry; Intestine, Small; Kidney; Liver; Membrane Proteins; Microbodies; Microscopy, Immunoelectron; Rats
PubMed: 7626801
DOI: 10.1002/jemt.1070310107