| Title: | Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis |
| ISSN/ISBN: | 0021-9525 (Print) 1540-8140 (Electronic) 0021-9525 (Linking) |
| Abstract: | "We describe an in vitro system with all components derived from the yeast Saccharomyces cerevisiae that can translocate a yeast secretory protein across microsomal membranes. In vitro transcribed prepro-alpha-factor mRNA served to program a membrane-depleted yeast translation system. Translocation and core glycosylation of prepro-alpha-factor were observed when yeast microsomal membranes were added during or after translation. A membrane potential is not required for translocation. However, ATP is required for translocation and nonhydrolyzable analogues of ATP cannot serve as a substitute. These findings suggest that ATP hydrolysis may supply the energy required for translocation of proteins across the endoplasmic reticulum" |
| Keywords: | "Adenosine Triphosphate/metabolism Biological Transport, Active Cell-Free System Endoplasmic Reticulum/*metabolism Fungal Proteins/*metabolism Glycoproteins/biosynthesis/metabolism Mating Factor Membrane Potentials Peptides/*metabolism Protein Biosynthesis;" |
| Notes: | "MedlineWaters, M G Blobel, G eng GM 07982/GM/NIGMS NIH HHS/ GM 27155/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1986/05/01 J Cell Biol. 1986 May; 102(5):1543-50. doi: 10.1083/jcb.102.5.1543" |
