Processing of Kex2 pro‐region at two interchangeable cleavage sites
- 24 May 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 323 (1-2) , 129-131
- https://doi.org/10.1016/0014-5793(93)81463-a
Abstract
In Saccharomyces cerevisiae, the Kex2 endoprotease (Kex2p) is required for the proteolytic maturation of α‐pheromone and also for the removal of its own pro‐region. Kex2p is specific for pairs of basic amino acid residues. Two putative processing sites are present in the pro‐region of Kexlp. We have expressed processing site mutants of Kex2p and assayed the production of active Kex2p. Mutations affecting either putative cleavage site do not alter the activity. However, mutations affecting both sites led to a reduction in both Kex2 activity and the amount of protein. These results suggest that removal of Kex2p pro‐peptide is required for the production of a stable enzyme and can occur at either processing site.Keywords
This publication has 12 references indexed in Scilit:
- Processing of Protein Precursors by a Novel Family of Subtilisin-Related Mammalian EndoproteasesNature Biotechnology, 1993
- The pro‐region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self‐processingFEBS Letters, 1992
- Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease.Proceedings of the National Academy of Sciences, 1992
- Kex2‐dependent processing of yeast K1 killer preprotoxin includes cleavage at ProArg‐44Molecular Microbiology, 1992
- Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway.The Journal of cell biology, 1991
- Prohormone Processing by Yeast ProteasesEnzyme, 1991
- The Yeast KEX-2-Processing Endoprotease Is Active in the Golgi Apparatus of Transfected NIH 3T3 FibroblastsMolecular Endocrinology, 1990
- A family of yeast expression vectors containing the phage f1 intergenic region1Gene, 1987
- Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factorCell, 1984
- Yeast α factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidaseCell, 1983