Localization of Dipeptidyl Aminopeptidase yscIV in the Plasma Membrane of Saccharomyces Cerevisiae
- 1 March 1990
- journal article
- research article
- Published by Microbiology Society in Journal of General Microbiology
- Vol. 136 (3) , 419-423
- https://doi.org/10.1099/00221287-136-3-419
Abstract
The subcellular distribution of dipeptidyl aminopeptidase activity was studied in protoplast lysates of Saccharomyces cerevisiae that were virtually free from vacuolar contamination. Dipeptidyl aminopeptidase yscIV, the STE13 gene product, was found to be associated with plasma membrane vesicles after sucrose gradient isopycnic centrifugation. Another dipeptidyl aminopeptidase activity, not yet fully characterized, was localized in a microvesicular population co-sedimenting with chitosomes.This publication has 12 references indexed in Scilit:
- Identification of the structural gene for dipeptidyl aminopeptidase yscV (DAP2) of Saccharomyces cerevisiaeJournal of Bacteriology, 1987
- Glycosylation and processing of prepro-α-factor through the yeast secretory pathwayCell, 1984
- Studies on the Regulation of X-Prolyl Dipeptidyl Aminopeptidase ActivityMicrobiology, 1983
- Yeast α factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidaseCell, 1983
- Control of yeast cell type by the mating type locusJournal of Molecular Biology, 1981
- α-d-mannosidase of Saccharomyces cerevisiae Characterization and modulation of activityBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- Proteolytic Activation and Inactivation of Chitin Synthetase from Mucor rouxiiJournal of General Microbiology, 1976
- Structure and transformation of chitin synthetase particles (chitosomes) during microfibril synthesis in vitro.Proceedings of the National Academy of Sciences, 1976
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Asymmetric distribution of Concanavalin A binding sites on yeast plasmalemma and vacuolar membraneArchiv für Mikrobiologie, 1976