Ergosteryl-β-glucosidase (Egh1) involved in sterylglucoside catabolism and vacuole formation in Saccharomyces cerevisiae

Takashi Watanabe, Motohiro Tani, Yohei Ishibashi, Ikumi Endo, Nozomu Okino, Makoto Ito

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Sterylglucosides (SGs) are composed of a glucose and sterol derivatives, and are distributed in fungi, plants and mammals. We recently identified EGCrP1 and EGCrP2 (endoglycoceramidase-related proteins 1 and 2) as a β-glucocerebrosidase and steryl-β-glucosidase, respectively, in Cryptococcus neoformans. We herein describe an EGCrP2 homologue (Egh1; ORF name, Yir007w) involved in SG catabolism in Saccharomyces cerevisiae. The purified recombinant Egh1 hydrolyzed various β-glucosides including ergosteryl β-glucoside (EG), cholesteryl β-glucoside, sitosteryl β-glucoside, para-nitrophenyl β-glucoside, 4-methylumberifellyl β-glucoside and glucosylceramide. The disruption of EGH1 in S. cerevisiae BY4741 (egh1Δ) resulted in the accumulation of EG and fragmentation of vacuoles. The expression of EGH1 in egh1Δ (revertant) reduced the accumulation of EG, and restored the morphology of vacuoles. The accumulation of EG was not detected in EGH1 and UGT51(ATG26) double-disrupted mutants (ugt51Δegh1Δ), indicating that EG was synthesized by Ugt51(Atg26) and degraded by Egh1 in vivo. These results clearly demonstrated that Egh1 is an ergosteryl-β-glucosidase that is functionally involved in the EG catabolic pathway and vacuole formation in S. cerevisiae.

Original languageEnglish
Pages (from-to)1079-1089
Number of pages11
JournalGlycobiology
Volume25
Issue number10
DOIs
Publication statusPublished - Apr 14 2015

All Science Journal Classification (ASJC) codes

  • Biochemistry

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