Abrogation of glucosidase I-mediated glycoprotein deglucosylation results in a sick phenotype in fission yeasts: Model for the human MOGS-CDG disorder.

ABSTRACT: Glucosidase I (GI) removes the outermost glucose from protein-linked Glc₃Man₉GlcNAc₂ (G3M9) in the endoplasmic reticulum (ER). Individuals with congenital disorders of glycosylation MOGS-CDG bear mutations in the GI-encoding gene (gls1). Although GI absence has been reported to produce lethality in Schizosaccharomyces pombe yeasts, here we obtained two viable Δgls1 mutants, one with a very sick but not lethal phenotype (Δgls1-S) and the other with a healthier one (Δgls1-H). The sick strain displayed only G3M9 as an ER protein-linked oligosaccharide, whereas the healthier strain had both G3M9 and Man₉GlcNAc₂ The lipid-linked oligosaccharide patterns of the two strains revealed that the most abundantly

SUBMITTER: Gallo GL 

PROVIDER: S-EPMC6311512 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature