UMMS Affiliation

Department of Biochemistry and Molecular Biology; Department of Biochemistry and Molecular Pharmacology

Date

11-17-1998

Document Type

Article

Subjects

Alleles; Chaperonins; Endoplasmic Reticulum; Fungal Proteins; Gene Expression Regulation, Fungal; Glycosylation; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins; Heat-Shock Proteins; Membrane Proteins; Mutagenesis; Oligosaccharides; Oxidative Stress; Protein Folding; RNA, Messenger; *Saccharomyces cerevisiae Proteins; Temperature; Yeasts

Disciplines

Biochemistry | Cell Biology | Molecular Biology | Pharmacology

Abstract

Members of the eukaryotic heat shock protein 70 family (Hsp70s) are regulated by protein cofactors that contain domains homologous to bacterial DnaJ. Of the three DnaJ homologues in the yeast rough endoplasmic reticulum (RER; Scj1p, Sec63p, and Jem1p), Scj1p is most closely related to DnaJ, hence it is a probable cofactor for Kar2p, the major Hsp70 in the yeast RER. However, the physiological role of Scj1p has remained obscure due to the lack of an obvious defect in Kar2p-mediated pathways in scj1 null mutants. Here, we show that the Deltascj1 mutant is hypersensitive to tunicamycin or mutations that reduce N-linked glycosylation of proteins. Although maturation of glycosylated carboxypeptidase Y occurs with wild-type kinetics in Deltascj1 cells, the transport rate for an unglycosylated mutant carboxypeptidase Y (CPY) is markedly reduced. Loss of Scj1p induces the unfolded protein response pathway, and results in a cell wall defect when combined with an oligosaccharyltransferase mutation. The combined loss of both Scj1p and Jem1p exaggerates the sensitivity to hypoglycosylation stress, leads to further induction of the unfolded protein response pathway, and drastically delays maturation of an unglycosylated reporter protein in the RER. We propose that the major role for Scj1p is to cooperate with Kar2p to mediate maturation of proteins in the RER lumen.

Rights and Permissions

Citation: J Cell Biol. 1998 Nov 16;143(4):921-33.

Related Resources

Link to Article in PubMed

Journal Title

The Journal of cell biology

PubMed ID

9817751

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