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Mol Cell Biol

Title:		Sec59 encodes a membrane protein required for core glycosylation in Saccharomyces cerevisiae
Author(s):		Bernstein M; Kepes F; Schekman R;
Address:		"Department of Biochemistry, University of California, Berkeley 94720"
Journal Title:		Mol Cell Biol
Year:		1989
Volume:		9
Issue:		3
Page Number:		1191 - 1199
DOI:		10.1128/mcb.9.3.1191-1199.1989
ISSN/ISBN:		0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
Abstract:		"When incubated at a restrictive temperature, Saccharomyces cerevisiae sec59 mutant cells accumulate inactive and incompletely glycosylated forms of secretory proteins. Three different secretory polypeptides (invertase, pro-alpha-factor, and pro-carboxypeptidase Y) accumulated within a membrane-bounded organelle, presumably the endoplasmic reticulum, and resisted proteolytic degradation unless the membrane was permeabilized with detergent. Molecular cloning and DNA sequence analysis of the SEC59 gene predicted an extremely hydrophobic protein product of 59 kilodaltons. This prediction was confirmed by reconstitution of the sec59 defect in vitro. The alpha-factor precursor, which was translated in a soluble fraction from wild-type cells, was translocated into, but inefficiently glycosylated within, membranes from sec59 mutant cells. Residual glycosylation activity of membranes of sec59 cells was thermolabile compared with the activity of wild-type membranes. Partial restoration of glycosylation was obtained in reactions that were supplemented with mannose or GDP-mannose, but not those supplemented with other sugar nucleotides. These results were consistent with a role for the Sec59 protein in the transfer of mannose to dolichol-linked oligosaccharide"
Keywords:		"Amino Acid Sequence Base Sequence Carboxypeptidases/genetics/metabolism Cathepsin A Cloning, Molecular DNA, Fungal/genetics Endoplasmic Reticulum/metabolism Fungal Proteins/*genetics/metabolism *Genes, Fungal Glycoside Hydrolases/genetics/metabolism Glyco;"
Notes:		"MedlineBernstein, M Kepes, F Schekman, R eng GM26755/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1989/03/01 Mol Cell Biol. 1989 Mar; 9(3):1191-9. doi: 10.1128/mcb.9.3.1191-1199.1989"