Yeast KEX2 protease and mannosyltransferase I are localized to distinct compartments of the secretory pathway
- 29 January 1989
- Vol. 5 (1) , 25-33
- https://doi.org/10.1002/yea.320050105
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‐α‐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.Keywords
This publication has 33 references indexed in Scilit:
- Yeast KEX2 Protease Has the Properties of a Human Proalbumin Converting EnzymeScience, 1987
- The trans Golgi Network: Sorting at the Exit Site of the Golgi ComplexScience, 1986
- Multiple Mechanisms of Protein Insertion into and Across MembranesScience, 1985
- Direct identification of prohormone conversion site in insulin-secreting cellsCell, 1985
- Attachment of terminal N-acetylglucosamine to asparagine-linked oligosaccharides occurs in central cisternae of the golgi stackCell, 1985
- Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factorCell, 1984
- Identification of coated vesicles in Saccharomyces cerevisiae.The Journal of cell biology, 1984
- Yeast α factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidaseCell, 1983
- Structure of a yeast pheromone gene (MFα): A putative α-factor precursor contains four tandem copies of mature α-factorCell, 1982
- Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuoleCell, 1982