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  • 1
    Electronic Resource
    Electronic Resource
    Peroxisome Biogenesis in the Yeast Hansenula polymorpha: A Structural and Functional Analysis (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 804 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb18607.x
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  • 2
    Electronic Resource
    Electronic Resource
    Studies on the effect of toxin T-514 on the integrity of peroxisomes in methylotrophic yeasts (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 91 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract We have studied the response of two methylotrophic yeasts (Hansenula polymorpha and Candida boidinii) to toxin T-514, a toxin lethal to man, extracted from the shrub Karwinska homboldtiana. Growth experiments indicated a dose-response effect; at enhanced concentrations (50 μg/ml) the different subcellular organelles rapidly disintegrated resulting in death of the cultures. At non-lethal concentrations (〈2μg/ml) growth ceased initially, but resumed after a lag period of 4 h. At the subcellular level a specific effect was observed on peroxisomal integrity. Distinct holes appeared in the peroxisomal membranes, resulting in leakage of matrix proteins from these organelles. In addition, import of newly synthesized proteins appeared to be blocked since cytosolic aggregates of matrix proteins were formed. The peroxisomal damage was probably irreversible since affected organelles were degraded at later stages of incubation. Upon restoration of growth on methanol, new peroxisomes developed from those which had escaped degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05210.x
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  • 3
    Electronic Resource
    Electronic Resource
    Sorting and function of peroxisomal membrane proteins (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 24 (2000), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Peroxisomes are subcellular organelles and are present in virtually all eukaryotic cells. Characteristic features of these organelles are their inducibility and their functional versatility. Their importance in the intermediary metabolism of cells is exemplified by the discovery of several inborn, fatal peroxisomal errors in man, the so-called peroxisomal disorders. Recent findings in research on peroxisome biogenesis and function have demonstrated that peroxisomal matrix proteins and peroxisomal membrane proteins (PMPs) follow separate pathways to reach their target organelle. This paper addresses the principles of PMP sorting and summarizes the current knowledge of the role of these proteins in organelle biogenesis and function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.2000.tb00543.x
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  • 4
    Electronic Resource
    Electronic Resource
    Neuropeptides and the microcircuitry of the enteric nervous system (1987)
    Springer
    Cellular and molecular life sciences 43 (1987), S. 813-821 
    Details
    ISSN: 1420-9071
    Keywords: Neuropeptides ; enteric nervous system ; intestine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The discovery of neuropeptides in enteric neurons has revolutionized the study of the microcircuitry of the enteric nervous system. Form immunohistochemistry, it is now clear that some individual enteric neurons contain several different neuropeptides with or without other transmitter-specific markers and that these markers occur in various combinations. There is evidence from experiments in which nerve pathways are interrupted that populations of enteric neurons with different combinations of markers have different projection patterns, sending their processes to distinct targets using different routes. Correlations between the neurochemistry of enteric neurons and the types of synaptic inputs they receive are also beginning to emerge from electrophysiological studies. These findings imply that enteric neurons are chemically coded by the combinations of peptides and other transmitter-related substances they contain and that the coding of each population correlates with its role in the neuronal pathways that control gastrointestinal function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01945359
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  • 5
    Electronic Resource
    Electronic Resource
    A new facile synthesis of 5-aryl-4-trifluoroacetyl-6-trifluoromethyl-3,4-dihydro-2H-1,3,4-oxadiazines from arylaldehydes
    Amsterdam : Elsevier
    Tetrahedron Letters 31 (1990), S. 1183-1184 
    Details
    ISSN: 0040-4039
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4039(00)88760-2
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of peroxisome-deficient mutants of Hansenula polymorpha (1995)
    Springer
    Current genetics 28 (1995), S. 248-257 
    Details
    ISSN: 1432-0983
    Keywords: Hansenula polymorpha ; Peroxisomes ; Organelle biogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the methylotrophic yeast Hansenula polymorpha, approximately 25% of all methanol-utilization-defective (Mut-) mutants are affected in genes required for peroxisome biogenesis (PER genes). Previously, we reported that one group of per mutants, termed Pim-, are characterized by the presence of a few small peroxisomes with the bulk of peroxisomal enzymes located in the cytosol. Here, we describe a second major group of per mutants that were observed to be devoid of any peroxisome-like structure (Per-). In each Per- mutant, the peroxisomal methanol-pathway enzymes alcohol oxidase, catalase and dihydroxyacetone synthase were present and active but located in the cytosol. Together, the Pim- and Per- mutant collections involved mutations in 14 different PER genes. Two of the genes, PER5 and PER7, were represented by both dominant-negative and recessive alleles. Diploids resulting from crosses of dominant per strains and wild-type H. polymorpha were Mut- and harbored peroxisomes with abnormal morphology. This is the first report of dominant-negative mutations affecting peroxisome biogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309784
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  • 7
    Electronic Resource
    Electronic Resource
    A Pichia pastoris VPS15 homologue is required in selective peroxisome autophagy (1999)
    Springer
    Current genetics 36 (1999), S. 262-269 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsPichia pastoris ; Peroxisome degradation ; Autophagy ; VPS15
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methylotrophic yeasts contain large peroxisomes during growth on methanol. Upon exposure to excess glucose or ethanol these organelles are selectively degraded by autophagy. Here we describe the cloning of a Pichia pastoris gene (PpVPS15) involved in peroxisome degradation, which is homologous to Saccharomyces cerevisiae VPS15. In methanol-grown cells of a P. pastoris VPS15 deletion strain, the levels of peroxisomal marker enzymes remained high after addition of excess glucose or ethanol. Electron microscopic studies revealed that the organelles were not taken up by vacuoles, suggesting that PpVPS15 is required at an early stage in peroxisome degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050499
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  • 8
    Electronic Resource
    Electronic Resource
    Methanol metabolism in a peroxisome-deficient mutant of Hansenula polymorpha: a physiological study (1991)
    Springer
    Archives of microbiology 156 (1991), S. 15-23 
    Details
    ISSN: 1432-072X
    Keywords: Hansenula polymorpha ; Peroxisomes ; Peroxisome function ; Peroxisome-deficient mutant ; Methanol metabolism ; Continuous cultures ; Mixed-substrates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have studied methanol-utilization in a peroxisome-deficient (PER) mutant of Hansenula polymorphoa. In spite of the fact that in carbon-limited chemostat cultures under induced conditions the enzymes involved in methanol metabolism were present at wild-type (WT) levels, this mutant is unable to grow on methanol as a sole carbon and energy source. Addition of methanol to glucose-limited (SR=12.5mM) chemostat cultures of the PER mutant only resulted in an increase in yield when small amounts were used (up to 22.5 mM). At increasing amounts however, a gradual decrease in cell density was observed which, at 80 mM methanol in the feed, had dropped below the original value of the glucose-limited culture. This reduction in yield was not observed when increasing amounts of formate instead of methanol were used as supplements for the glucose-limited mutant culture and also not in WT cells, used as control in these experiments. The effect of addition of methanol to a glucose-limited PER culture was also studied in the transient state during adaptation of the cells to methanol. The enzyme patterns obtained suggested that the ultimate decrease in yield observed at enhanced methanol concentrations was due to an inefficient methanolmetabolism as a consequence of the absence of peroxisomes. The absence of intact peroxisomes results in two major problems namely i) in H2O2-metabolism, which most probably is no longer mediated by catalase and ii) the inability of the cell to control the fluxes of formaldehyde, generated from methanol. The energetic consequences of this metabolism, compared to the WT situation with intact peroxisomes, are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00418181
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  • 9
    Electronic Resource
    Electronic Resource
    Growth of catalase A and catalase T deficient mutant strains of Saccharomyces cerevisiae on ethanol and oleic acid (1990)
    Springer
    Archives of microbiology 153 (1990), S. 513-517 
    Details
    ISSN: 1432-072X
    Keywords: Saccharomyces cerevisiae ; Catalase A ; Catalase T ; β-Oxidation ; Microbodies ; H2O2-Metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The parental strain (A+T+) of Saccharomyces cerevisiae and mutants, deficient in catalase T (A+T−), catalase A (A−T+) or both catalases (A−T−), grew on ethanol and oleic acid with comparable doubling times. Specific activities of catalase were low in glucose- and ethanol-grown cells. In the two oleic acid-grown A+-strains (A+T+ and A+T−) high catalase activities were found; catalase activity invariably remained low in the A−T+ strain and was never detected in the A−T− strain. The levels of β-oxidation enzymes in oleic acid-grown cells of the parental and all mutant strains were not significantly different. However, cytochrome C peroxidase activity had increased 8-fold in oleic acid grown A− strains (A−T+ and A−T−) compared to parental strain cells. The degree of peroxisomal proliferation was comparable among the different strains. Catalase A was shown to be located in peroxisomes. Catalase T is most probably cytosolic in nature and/or present in the periplasmic space.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248436
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  • 10
    Electronic Resource
    Electronic Resource
    In vivo inactivation of peroxisomal alcohol oxidase in Hansenula polymorpha by KCN is an irreversible process (1988)
    Springer
    Archives of microbiology 151 (1988), S. 26-33 
    Details
    ISSN: 1432-072X
    Keywords: Hansenula polymorpha ; Peroxisomes ; Alcohol oxidase ; Protein assemblage ; FAD ; Cyanide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The fate of alcohol oxidase (AO) in chemostatgrown cells of Hansenula polymorpha, after its inactivation by KCN, was studied during subsequent cultivation of the cyanide-treated cells in fresh methanol media. Biochemical experiments showed that the cyanide-induced inactivation of AO was due to the release of flavin adenine dinucleotide (FAD) from the holo enzyme. However, dissociation of octameric AO into subunits was not observed. Subsequent growth of intact cyanide-treated cells in fresh methanol media was paralelled by proteolytic degradation of part of the peroxisomes present in the cells. The recovery of AO activity, concurrently observed in these cultures, was accounted for by synthesis of new enzyme protein. Reactivation of previously inactivated AO was not observed, even in the presence of FAD in such cultures. Newly synthesized AO protein was incorporated in only few of the peroxisomes present in the cells. 31P nuclear magnetic resonance (NMR) studies showed that cyanide-treatment of the cells led to a dissipation of the pH gradient across the peroxisomal membrane. However, restoration of this pH gradient was fast when cells were incubated in fresh methanol medium after removal of the cyanide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00444664
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