RRC ID 72799
Author Tanaka N, Kagami A, Hirai K, Suzuki S, Matsuura S, Fukunaga T, Tabuchi M, Takegawa K.
Title The fission yeast gmn2+ gene encodes an ERD1 homologue of Saccharomyces cerevisiae required for protein glycosylation and retention of luminal endoplasmic reticulum proteins.
Journal J Gen Appl Microbiol
Abstract 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 Gmn2-EGFP 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.
Volume 67(2)
Pages 67-76
Published 2021-6-3
DOI 10.2323/jgam.2020.07.002
PMID 33536395
MeSH Amino Acid Sequence Endoplasmic Reticulum / metabolism* Glycosylation Glycosyltransferases / metabolism Golgi Apparatus / metabolism Kluyveromyces / genetics Membrane Proteins / genetics Membrane Proteins / metabolism* Mutation Open Reading Frames Saccharomyces cerevisiae / genetics Schizosaccharomyces / genetics Schizosaccharomyces / metabolism* Schizosaccharomyces pombe Proteins / genetics Schizosaccharomyces pombe Proteins / metabolism*
IF 1.442
Yeast pAL-KS pAU-KS