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. 1986 May 1;102(5):1543–1550. doi: 10.1083/jcb.102.5.1543

Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis

PMCID: PMC2114218  PMID: 3517001

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.

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Selected References

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