| Title: | Glycosylation and processing of prepro-alpha-factor through the yeast secretory pathway |
| Author(s): | Julius D; Schekman R; Thorner J; |
| DOI: | 10.1016/0092-8674(84)90224-1 |
| ISSN/ISBN: | 0092-8674 (Print) 0092-8674 (Linking) |
| Abstract: | "Events in the synthesis and processing of prepro-alpha-factor have been assessed with the aid of mutants blocked at various stages in the yeast secretory pathway. In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec 18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5)" |
| Keywords: | "Genotype Glycoside Hydrolases/metabolism Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Mating Factor Peptides/*genetics Protein Biosynthesis Protein Precursors/*genetics *Protein Processing, Post-Translational RNA, Messenger/genetics Saccharomyc;" |
| Notes: | "MedlineJulius, D Schekman, R Thorner, J eng Research Support, U.S. Gov't, P.H.S. 1984/02/01 Cell. 1984 Feb; 36(2):309-18. doi: 10.1016/0092-8674(84)90224-1" |
