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Yeast KEX2 protease and mannosyltransferase I are localized to distinct compartments of the secretory pathway
Author(s) -
Cunningham Kyle W.,
Wickner William T.
Publication year - 1989
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320050105
Subject(s) - biology , protease , saccharomyces cerevisiae , biochemistry , golgi apparatus , yeast , intracellular , enzyme , microbiology and biotechnology , cell
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.