Evidence for functional heterogeneity among microbodies in yeasts View Full Text


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Article Info

DATE

1989-01

AUTHORS

Marten Veenhuis, Grietje Sulter, Ida van der Klei, Wim Harder

ABSTRACT

We have studied the biogenesis and enzymic composition of microbodies in different yeasts during adaptation of cells to a new growth environment. After a shift of cells of Candida boidinii and Hansenula polymorpha from glucose to methanol/methylamine-containing media, newly synthesized alcohol oxidase and amine oxidase are imported in one and the same organelle together with catalase; as a consequence the cells contain one class of morphologically and enzymatically identical microbodies. Similar results were obtained when Candida utilis cells were transferred from glucose to ethanol/ethylamine-containing media upon which all cells formed microbodies containing amine oxidase and catalase. However, when methanol-limited cells of H. polymorpha were transferred from media containing ammonium sulphate to those with methylamine as the nitrogen source, newly synthesized amine oxidase was incorporated only in part of the microbodies present in these cells. This uptake was confined to the few smaller organelles generally present at the perimeter of the cells, which were considered not fully developed (immature) as judged by their size. Essentially similar results were obtained when stationary phase cells of C. boidinii or C. utilis - grown on methanol and ethanol plus ammonium sulphate, respectively - were shifted to media containing (m)ethylamine as the nitrogen source. These results indicate that mature microbodies may exist in yeasts which no longer are involved in the uptake of matrix proteins. Therefore, these yeasts may display heterogeneities in their microbody population. More... »

PAGES

105-110

References to SciGraph publications

  • 1978-05. Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymorpha and its relation to environmental conditions in ARCHIVES OF MICROBIOLOGY
  • 1981-03. Biogenesis and turnover of peroxisomes involved in the concurrent oxidation of methanol and methylamine in Hansenula polymorpha in ARCHIVES OF MICROBIOLOGY
  • 1973-01. Controlled Nucleation for the Regulation of the Particle Size in Monodisperse Gold Suspensions in NATURE
  • 1979-02. Characterization of peroxisomes in glucose-grown Hansenula polymorpha and their development after the transfer of cells into methanol-containing media in ARCHIVES OF MICROBIOLOGY
  • 1964-07. Die Gefrier-Fixation lebender Zellen und ihre Anwendung in der Elektronenmikroskopie in CELL AND TISSUE RESEARCH
  • 1987-03. A 31P NMR study of the internal pH of yeast peroxisomes in ARCHIVES OF MICROBIOLOGY
  • 1987-03. A proton-translocating adenosine triphosphatase is associated with the peroxisomal membrane of yeasts in ARCHIVES OF MICROBIOLOGY
  • 1985-01. Biogenesis and metabolic significance of microbodies in urate-utilizing yeasts in ANTONIE VAN LEEUWENHOEK
  • 1976-12. Cytochemical studies on the localization of methanol oxidase and other oxidases in peroxisomes of methanol-grown Hansenula polymorpha in ARCHIVES OF MICROBIOLOGY
  • 1987. Metabolic Significance and Biogenesis of Microbodies in Yeasts in PEROXISOMES IN BIOLOGY AND MEDICINE
  • 1976-12. Growth of Hansenula polymorpha in a methanol-limited chemostat in ARCHIVES OF MICROBIOLOGY
  • 1980-06. Development of amine oxidase-containing peroxisomes in yeasts during growth on glucose in the presence of methylamine as the sole source of nitrogen in ARCHIVES OF MICROBIOLOGY
  • 1986-06. Physiological role of microbodies in the yeast Trichosporon cutaneum during growth on ethylamine as the source of energy, carbon and nitrogen in ARCHIVES OF MICROBIOLOGY
  • 1975-01. Cytochemical localization of catalase activity in methanol-grown Hansenula polymorpha in ARCHIVES OF MICROBIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00414422

    DOI

    http://dx.doi.org/10.1007/bf00414422

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1007937407

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/2655547


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