| Title: | Secretion in yeast: translocation and glycosylation of prepro-alpha-factor in vitro can occur via an ATP-dependent post-translational mechanism |
| Address: | "Cell Biology Program, European Molecular Biology Laboratory, 6900 Heidelberg, FRG" |
| DOI: | 10.1002/j.1460-2075.1986.tb04318.x |
| ISSN/ISBN: | 0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking) |
| Abstract: | "In an in vitro system comprising a yeast cell-free translation system, yeast microsomes and mRNA encoding prepro-alpha-factor, the translocation of this protein across the membrane of the microsomal vesicle and its glycosylation could b uncoupled from its translation. Such post-translational processing is dependent upon the presence of ATP in the system. It is not, however, affected by a variety of uncouplers, ionophores or inhibitors, including carbonyl cyanide m-chlorophenyl hydrazone (CCCP), valinomycin, nigericin, dinitrophenol (DNP), potassium cyanide (KCN) or N-ethyl maleimide (NEM). This mechanism of translocation is significant as it indicates that a protein of 18 000 daltons is capable of crossing an endoplasmic reticulum-derived membrane post-translationally. For the moment, this phenomenon seems to be restricted to prepro-alpha-factor in the yeast in vitro system. Neither invertase nor IgG chi light chain could be translocated post-translationally in yeast, nor was such processing observed for prepro-alpha-factor in a wheat germ system supplemented with canine pancreatic microsomes" |
| Keywords: | "Adenosine Triphosphate/metabolism Endoplasmic Reticulum/metabolism Glycosylation Mating Factor Peptides/*metabolism Protein Precursors/*metabolism *Protein Processing, Post-Translational *Protein Transport Saccharomyces cerevisiae/*metabolism Saccharomyce;" |
| Notes: | "MedlineRothblatt, J A Meyer, D I eng Research Support, Non-U.S. Gov't England 1986/05/01 EMBO J. 1986 May; 5(5):1031-6. doi: 10.1002/j.1460-2075.1986.tb04318.x" |
