title: Yeast KEX2 protease and mannosyltransferase I are localized to distinct compartments of the secretory pathway.
abstract: The KEX2 protease (product of the KEX2 gene) functions late in the secretory pathway of Saccharomyces cerevisiae by cleaving the polypeptide chains of prepro-killer toxin and prepro-alpha-factor at paired basic amino acid residues. The intracellular vesicles containing KEX2 protease sedimented in density gradients to a position distinct from those containing mannosyltransferase I (product of the MNN1 gene), a marker enzyme for the Golgi complex. The recovery of intact compartments containing these enzymes approached 80% after sedimentation. We propose that the KEX2 protease and mannosyltransferase I reside within distinct compartments.
authors.affiliation: Molecular Biology Institute, University of California, Los Angeles 90024.
authors.forename: K W
authors.initials: KW
authors.lastname: Cunningham
authors.forename: W T
authors.initials: WT
authors.lastname: Wickner
mesh_terms: D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D002854:Chromatography, Paper; D003594:Cytoplasmic Granules / Q000201:enzymology*; D006056:Golgi Apparatus / Q000201:enzymology; D006602:Hexosyltransferases / Q000032:analysis*; D008364:Mannosyltransferases / Q000032:analysis*; D043484:Proprotein Convertases; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000032:analysis*; D013381:Subtilisins
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D006602:Hexosyltransferases; D008364:Mannosyltransferases; D043484:Proprotein Convertases; D012697:Serine Endopeptidases; D013381:Subtilisins; C058751:KEX2 protein, S cerevisiae