The fission yeast gmn2+ gene encodes an erd1 homologue of saccharomyces cerevisiae required for protein glycosylation and retention of luminal endoplasmic reticulum proteins

Naotaka Tanaka, Akinari Kagami, Keisuke Hirai, Shotaro Suzuki, Shiori Matsuura, Takamasa Fukunaga, Mitsuaki Tabuchi, Kaoru Takegawa

研究成果: Contribution to journalArticle査読

抄録

The gmn2 mutant of Schizosaccharomyces pombe has previously been shown to exhibit defects in protein glycosylation of N-linked oligosaccharides (Ballou, L. and Ballou, CE., Proc. Natl. Acad. Sci. USA, 92, 2790–2794 (1995)). Like most glycosylation-defective mutants, the S. pombe gmn2 mutant was found to be sensitive to hygromycin B, an aminoglycoside antibiotic. As a result of complementation analysis, the gmn2+ gene was found to be a single open reading frame that encodes a polypeptide of 373 amino acids consisting of multiple membrane-spanning regions. The Gmn2 protein shares sequence similarity with Kluyveromyces lactis and Saccharomyces cerevisiae Erd1 proteins, which are required for retention of luminal endoplasmic reticulum (ER) proteins. Although disruption of the gmn2+ gene is not lethal, the secreted glycoprotein showed a significant glycosylation defect with destabilization of the glycosyltransferase responsible for N-glycan elongation. It was also shown that a significant amount of BiP was missorted to the cell surface according to ADEL receptor destabilization. Fluorescent microscopy revealed that the functional Gmn2EGFP fusion protein is mainly localized in the Golgi membrane. These results indicate that the Gmn2 protein is required for protein glycosylation and for retention of ER-resident proteins in S. pombe cells.

本文言語英語
ページ(範囲)67-76
ページ数10
ジャーナルJournal of General and Applied Microbiology
67
2
DOI
出版ステータス出版済み - 2021

All Science Journal Classification (ASJC) codes

  • 微生物学
  • 応用微生物学とバイオテクノロジー

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