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  • 1
    Electronic Resource
    Electronic Resource
    Biogenesis and turnover of peroxisomes involved in the concurrent oxidation of methanol and methylamine in Hansenula polymorpha (1981)
    Springer
    Archives of microbiology 129 (1981), S. 35-41 
    Details
    ISSN: 1432-072X
    Keywords: Peroxisome ; Methanol ; Methylamine ; Yeast ; Hansenula polymorpha ; Alcohol oxidase ; Amino oxidase ; Catalase ; Catabolite inactivation ; Turnover ; Cytochemical localization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Growth of Hansenula polymorpha in shake flasks and chemostat cultures in the presence of methanol as the sole source of carbon and methylamine as the sole source of nitrogen was associated with the development of peroxisomes in the cells. The organelles were involved in the concurrent oxidation of these two compounds, since they contained both alcohol oxidase and amine oxidase, which are key enzymes in methanol and methylamine metabolism, respectively. In addition catalase was present. Peroxisomes with a completely crystalline substructure were observed in methanol-limited chemostat-grown cells. Amine oxidase probably formed an integral part of these crystalloids, whereas catalase was present in a freely diffusable form. Transfer of cells, grown in a methanol-limited chemostat in the presence of methylamine into glucose/ammonium sulphate media resulted in the loss of both alcohol oxidase and amine oxidase activity from the cells. This process was associated with degradation of the crystalline peroxisomes. However, when cells were transferred into glucose/methylamine media, amine oxidase activity only declined during 2 h after the transfer and thereafter increased again. This subsequent rise in amine oxidase activity was associated with the development of new peroxisomes in the cells in which degradation of the crystalline peroxisomes, originally present, continued. These newly formed organelles probably originated from peroxisomes which had not been affected by degradation. When in the methanollimited chemostat methylamine was replaced by ammonium sulphate, repression of the synthesis of amine oxidase was observed. However, inactivation of this enzyme or degradation of peroxisomes was not detected. The decrease of amine oxidase activity in the culture was accounted for by dilution of enzyme as a result of growth and washout.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00417176
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  • 2
    Electronic Resource
    Electronic Resource
    A proton-translocating adenosine triphosphatase is associated with the peroxisomal membrane of yeasts (1987)
    Springer
    Archives of microbiology 147 (1987), S. 42-47 
    Details
    ISSN: 1432-072X
    Keywords: Hansenula polymorpha ; Yeast ; Peroxisomes ; Proton-translocating ATPase ; Cell fractionation ; Fluorescence quenching studies ; Cytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The association of an ATPase with the yeast peroxisomal membrane was established by both biochemical and cytochemical procedures. Peroxisomes were purified from protoplast homogenates of the methanol-grown yeast Hansenula polymorpha by differential and sucrose gradient centrifugation. Biochemical analysis revealed that ATPase activity was associated with the peroxisomal peak fractions which were identified on the basis of alcohol oxidase and catalase activity. The properties of this ATPase closely resembled those of the mitochondrial ATPase of this yeast. The enzyme was Mg2+-dependent, had a pH optimum of approximately 8.5 and was sensitive to N,N′-dicyclohexylcarbodiimide (DCCD), oligomycin and azide, but not to vanadate. A major difference was the apparent K m for ATP which was 4–6 mM for the peroxisomal ATPase compared to 0.6–0.9 mM for the mitochondrial enzyme. Cytochemical experiments indicated that the peroxisomal ATPase was associated with the membranes surrounding these organelles. After incubations with CeCl3 and ATP specific reaction products were localized on the peroxisomal membrane, both when unfixed isolated peroxisomes or formaldehyde-fixed protoplasts were used. This staining was strictly ATP-dependent; in controls performed i) in the absence of substrate, ii) in the presence of glycerol 2-phosphate instead of ATP, or iii) in the presence of DCCD, staining was invariably absent. Similar staining patterns were observed in subcellular fractions and protoplasts of Candida utilis and Trichosporon cutaneum X4, grown in the presence of ethanol/ethylamine or ethylamine, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00492903
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  • 3
    Electronic Resource
    Electronic Resource
    Permeability properties of peroxisomal membranes from yeasts (1990)
    Springer
    Archives of microbiology 153 (1990), S. 490-495 
    Details
    ISSN: 1432-072X
    Keywords: Hansenula polymorpha ; Candida boidinii ; Peroxisome ; Peroxisomal membrane ; Permeability ; Membrane fusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have studied the permeability properties of intact peroxisomes and purified peroxisomal membranes from two methylotrophic yeasts. After incorporation of sucrose and dextran in proteoliposomes composed of asolectin and peroxisomal membranes isolated from the yeasts Hansenula polymorpha and Candida boidinii a selective leakage of sucrose occurred indicating that the peroxisomal membranes were permeable to small molecules. Since the permeability of yeast peroxisomal membranes in vitro may be due to the isolation procedure employed, the osmotic stability of peroxisomes was tested during incubations of intact protoplasts in hypotonic media. Mild osmotic swelling of the protoplasts also resulted in swelling of the peroxisomes present in these cells but not in a release of their matrix proteins. The latter was only observed when the integrity of the cells was disturbed due to disruption of the cell membrane during further lowering of the concentration of the osmotic stabilizer. Stability tests with purified peroxisomes indicated that this leak of matrix proteins was not associated with the permeability to sucrose. Various attempts to mimic the in vivo situation and generate a proton motive force across the peroxisomal membranes in order to influence the permeability properties failed. Two different proton pumps were used for this purpose namely bacteriorhodopsin (BR) and reaction center-light-harvesting complex I (RCLHI complex). After introduction of BR into the membrane of intact peroxisomes generation of a pH-gradient was not or barely detectable. Since this pump readily generated a pH-gradient in pure liposomes, these results strengthened the initial observations on the leakiness of the peroxisomal membrane fragments. Generation of a membrane potential (Δψ) was also not observed when RCLHI complex was introduced into vesicles of purified peroxisomal membranes. The significance of the observed permeability of isolated yeast peroxisomal membranes to small molecules with respect to current and future in vitro import studies is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248432
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of peroxisomes in glucose-grown Hansenula polymorpha and their development after the transfer of cells into methanol-containing media (1979)
    Springer
    Archives of microbiology 120 (1979), S. 167-175 
    Details
    ISSN: 1432-072X
    Keywords: Peroxisome ; Biogenesis ; Yeast ; Hansenula polymorpha ; Cytochemical staining ; Methanol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cells of Hansenula polymorpha growing exponentially on glucose generally contained a single peroxisome of small dimension, irregular in shape and located in close proximity to the cell wall. Crystalline inclusions in the peroxisomal matrix were not observed. Associations of the organelles with one or more strands of endoplasmic reticulum were evident. In stationary phase cells the size of the peroxisomes had increased considerably. They were more cubical in form and showed a partly or completely crystalline matrix. After the transfer of cells growing exponentially on glucose into media containing methanol, large peroxisomes with a partly crystalline matrix developed in the cells within 6 h. These organelles originated from the small peroxisomes in the glucose-grown cells. De novo synthesis of peroxisomes was not observed. Prolonged cultivation in the presence of methanol resulted in a gradual increase in the number of peroxisomes by means of separation of small peroxisomes from mature organelles. During growth of peroxisomes associations with the endoplasmic reticulum remained evident. The increase in volume density of peroxisomes in stationary phase cells grown on glucose and in methanol-grown cells was accompanied by the synthesis of the peroxisomal enzymes alcohol oxidase and catalase. Cytochemical staining techniques revealed that alcohol oxidase activity was only detected when the peroxisomes contained a crystalloid inclusion. Since in peroxisomes of an alcohol oxidase-negative mutant of Hansenula polymorpha crystalline inclusions were never detected, it is concluded that the development of crystalloids inside peroxisomes is due to the accumulation of alcohol oxidase in these organelles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409104
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  • 5
    Electronic Resource
    Electronic Resource
    Cytochemical studies on the localization of methanol oxidase and other oxidases in peroxisomes of methanol-grown Hansenula polymorpha (1976)
    Springer
    Archives of microbiology 111 (1976), S. 123-135 
    Details
    ISSN: 1432-072X
    Keywords: Cytochemical localization ; Peroxisome ; Catalase ; Methanol oxidase ; d-Amino acid oxidase ; α-Hydroxyacid oxidase ; Methanol-assimilating yeast ; Hansenula polymorpha
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The localization of methanol oxidase activity in cells of methanol-limited chemostat cultures of the yeast Hansenula polymorpha has been studied with different cytochemical staining techniques. The methods were based on enzymatic or chemical trapping of the hydrogen peroxide produced by the enzyme during aerobic incubations of whole cells in methanol-containing media. The results showed that methanol-dependent hydrogen peroxide production in either fixed or unfixed cells exclusively occurred in peroxisomes, which characteristically develop during growth of this yeast on methanol. Apart from methanol oxidase and catalase, the typical peroxisomal enzymes d-aminoacid oxidase and l-α-hydroxyacid oxidase were also found to be located in the peroxisomes. Urate oxidase was not detected in these organelles. Phase-contrast microscopy of living cells revealed the occurrence of peroxisomes which were cubic of form. This unusual shape was also observed in thin sections examined by electron microscopy. The contents of the peroxisomes showed, after various fixation procedures, a completely crystalline or striated substructure. It is suggested that this substructure might represent the in vivo organization structure of the peroxisomal enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446559
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  • 6
    Electronic Resource
    Electronic Resource
    Methanol metabolism in yeasts: Regulation of the synthesis of catabolic enzymes (1980)
    Springer
    Archives of microbiology 124 (1980), S. 115-121 
    Details
    ISSN: 1432-072X
    Keywords: Derepression ; Catabolite inactivation ; Alcohol oxidase ; Catalase ; Formaldehyde dehydrogenase ; Formate dehydrogenase ; Hansenula polymorpha ; Kloeckera sp. 2201 ; Peroxisomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulation of the synthesis of four dissimilatory enzymes involved in methanol metabolism, namely alcohol oxidase, formaldehyde dehydrogenase, formate dehydrogenase and catalase was investigated in the yeasts Hansenula polymorpha and Kloeckera sp. 2201. Enzyme profiles in cell-free extracts of the two organisms grown under glucose limitation at various dilution rates, suggested that the synthesis of these enzymes is controlled by derepression — represion rather than by induction — repression. Except for alcohol oxidase, the extent to which catabolite repression of the catabolic enzymes was relieved at low dilution rates was similar in both organisms. In Hansenula polymorpha the level of alcohol oxidase in the cells gradually increased with decreasing dilution rate, whilst in Kloeckera sp. 2201 derepression of alcohol oxidase synthesis was only observed at dilution rates below 0.10 h−1 and occurred to a much smaller extent than in Hansenula polymorpha. Derepression of alcohol oxidase and catalase in cells of Hansenula polymorpha was accompanied by synthesis of peroxisomes. Moreover, peroxisomes were degraded with a concurrent loss of alcohol oxidase and catalase activities when excess glucose was introduced into the culture. This process of catabolite inactivation of peroxisomal enzymes did not affect cytoplasmic formaldehyde dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00427715
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of glyoxysomes in yeasts and their transformation into peroxisomes in response to changes in environmental conditions (1983)
    Springer
    Archives of microbiology 136 (1983), S. 28-38 
    Details
    ISSN: 1432-072X
    Keywords: Yeasts ; Candida utilis ; Hansenula polymorpha ; Microbodies ; Peroxisomes ; Glyoxysomes ; Cell fractionation ; Cytochemistry ; Catalase ; Glyoxylate cycle ; Oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During growth of the yeasts Candida utilis and Hansenula polymorpha in mineral media containing ethanol as a carbon source and ammonium sulphate as a nitrogen source, the specific activities of isocitrate lyase and malate synthase were significantly increased when compared to glucose/ammonium sulphate-grown cells. In addition to the enhanced levels of these glyoxylate cycle enzymes, an increase in the specific activities of d-amino acid oxidase, amine oxidase or urate oxidase was observed when ammonium sulphate in the ethanol medium was replaced by d-alanine, methyl- or ethylamine, or uric acid. The subcellular localization of these enzymes was investigated by cell fractionation studies involving homogenization of protoplasts followed by differential and sucrose gradient centrifugation. In ethanol/ammonium sulphate-grown cells, isocitrate lyase and malate synthase cosedimented in a fraction together with catalase and part of the malate dehydrogenase. Electron microscopy revealed that this fraction consisted of microbodies which must be regarded as glyoxysomes. Two other glyoxylate cycle enzymes, citrate synthase and aconitase together with the other part of malate dehydrogenase, cosedimented with cytochrome c oxidase, a mitochondrial marker enzyme. In ethanol/d-alanine-, ethanol/methylamine- or ethanol/ethylamine-grown C. utilis and ethanol/uric acid-grown H. polymorpha, a peroxisomal enzyme, i.e. d-amino acid oxidase, amine oxidase or uric acid oxidase cosedimented with the glyoxysomal key enzymes. Cytochemical staining experiments demonstrated that in these variously-grown cells the activities of the oxidases were confined to the microbodymatrix; this also contained malate synthase activity. Transfer of C. utilis cells from glucose/ammonium sulphate- into ethanol/ammonium sulphate-containing media resulted in an increase in the original size and volume fraction of the microbodies. A further increase was observed when ammonium sulphate was replaced by methylamine. Essentially similar results were obtained with H. polymorpha cells. In neither of the two organisms indications of de novo synthesis of microbodies was obtained during transfer experiments. Invariably the microbodies developing in cells placed in the new environment originated from organelles already present in the inoculum cells by import of the substratespecific enzyme protein(s). The combined results of biochemical, cytochemical and electron microscopical experiments showed that in the yeasts studied under appropriate conditions glyoxysomal and peroxisomal enzyme activities were localized in one and the same microbody, rather than in separate organelles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00415606
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  • 8
    Electronic Resource
    Electronic Resource
    Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymorpha and its relation to environmental conditions (1978)
    Springer
    Archives of microbiology 117 (1978), S. 153-163 
    Details
    ISSN: 1432-072X
    Keywords: Peroxisome ; Methanol ; Cytochemical staining ; Yeast ; Hansenula polymorpha
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The development of peroxisomes has been studied in cells of the yeast Hansenula polymorpha during growth on methanol in batch and chemostat cultures. During bud formation, new peroxisomes were generated by the separation of small peroxisomes from mature organelles in the mother cells. The number of peroxisomes migrating to the buds was dependent upon environmental conditions. Aging of cells was accompanied by an increase in size of the peroxisomes and a subsequent increase in their numbers per cell. Their ultimate shape and substructure as well as their number per cell was dependent upon the physiological state of the culture. The change in number and volume density of peroxisomes was related to the level of alcohol oxidase in the cells. Development of peroxisomes in cells of batch cultures was accompanied by an increase in size of the crystalline inclusions in the organelles; they had become completely crystalline when the cells were in the stationary phase. Peroxisomes in cells from methanol-limited chemostat cultures were completely crystalline, irrespective of growth rate. Results of biochemical and cytochemical experiments suggested that alcohol oxidase is a major component of the crystalline inclusions in the peroxisomes of methanol-grown Hansenula polymorpha. Possible mechanisms involved in the ultrastructural changes in peroxisomes during their development have been discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402303
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  • 9
    Electronic Resource
    Electronic Resource
    Development of amine oxidase-containing peroxisomes in yeasts during growth on glucose in the presence of methylamine as the sole source of nitrogen (1980)
    Springer
    Archives of microbiology 126 (1980), S. 117-126 
    Details
    ISSN: 1432-072X
    Keywords: Candida utilis ; Hansenula polymorpha ; Amine oxidase ; Methylamine ; Nitrogen metabolism ; Peroxisome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The metabolism of methylamine as the nitrogen source for growth of the non-methylotrophic yeast Candida utilis and the methylotrophic yeast Hansenula polymorpha was investigated. Grwoth of both organisms in media with glucose and methylamine was associated with the presence of an amine oxidase in these cells. The enzyme catalyses the oxidation of methylamine by molecular oxygen into ammonia, formaldehyde and hydrogen peroxide and it is considered to be the key enzyme in methylamine metabolism in the organisms studied. In addition to synthesis of amine oxidase, derepression of catalase, formaldehyde and formate dehydrogenase was also observed upon transfer of cells of the two organisms from media containing ammonium ions into media containing methylamine as the nitrogen source. The synthesis of enzymes was paralleled by the development of a number of large microbodies in the cells. Cytochemical staining experiments indicated that the amine oxidase activity was located in the microbodies in both organisms. Catalase-activity was also demonstrated in these organelles, which can therefore be considered as peroxisomes. The present contribution is the first description of a peroxisomal amine oxidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00511216
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  • 10
    Electronic Resource
    Electronic Resource
    Watermelon glyoxysomal malate dehydrogenase is sorted to peroxisomes of the methylotrophic yeast, Hansenula polymorpha
    Amsterdam : Elsevier
    FEBS Letters 334 (1993), S. 128-132 
    Details
    ISSN: 0014-5793
    Keywords: Citrullus vulgaris ; Glyoxysome ; Hansenula polymorpha ; Malate dehydrogenase ; Peroxisome ; Protein targeting
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81697-X
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