Multiple functions of ergosterol in the fission yeast Schizosaccharomyces pombe

Tomoko Iwaki, Haruyuki Iefuji, Yoshikazu Hiraga, Akira Hosomi, Tomotake Morita, Yuko Giga-Hama, Kaoru Takegawa

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Sterols are a major class of membrane lipids in eukaryotes. In Schizosaccharomyces pombe, sterol 24-C-methyltransferase (Erg6p), C-8 sterol isomerase (Erg2p), C-5 sterol desaturase (Erg31p, Erg32p), C-22 sterol desaturase (Erg5p) and C-24 (28) sterol reductase (Sts1p/Erg4p) have been predicted, but not yet determined, to catalyse a sequence of reactions from zymosterol to ergosterol. Disruption mutants of these genes were unable to synthesize ergosterol, and most were tolerant to the polyene drugs amphotericin B and nystatin. Disruption of erg31+ or erg32+ did not cause ergosterol deficiency or tolerance to polyene drugs, indicating that the two C-5 sterol desaturases have overlapping functions. GFP-tagged DRM (detergent-resistant membrane)-associated protein Pma1p localized to the plasma membrane in ergΔ mutants. DRM fractionation revealed that the association between Pma1-GFP and DRM was weakened in erg6Δ but not in other erg mutants. Several GFP-tagged plasma membrane proteins were tested, and an amino acid permease homologue, SPBC359.03c, was found to mislocalize to intracellular punctate structures in the ergA mutants. These results indicate that these proteins are responsible for ergosterol biosynthesis in fission yeast, similar to the situation in Saccharomyces cerevisiae. Furthermore, in fission yeast, ergosterol is important for plasma membrane structure and function and for localization of plasma membrane proteins.

Original languageEnglish
Pages (from-to)830-841
Number of pages12
JournalMicrobiology
Volume154
Issue number3
DOIs
Publication statusPublished - Mar 2008

All Science Journal Classification (ASJC) codes

  • Microbiology

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