Abstract
Signal sequences of Saccharomyces cerevisiae invertase and alpha-factor pheromone were tested for the ability to mediate protein transport through the inner membrane of Escherichia coli by fusion to bacterial beta-lactamase lacking the signal sequence (blaS0). Both types of transformants exhibited ampicillin resistance in accordance with the transport of the fused protein to the periplasmic compartment. This compartment contained most of the beta-lactamase activity present in the cell. Therefore, the tested yeast signal sequences, which conferred translocation of their proteins across the membrane of the endoplasmic reticulum in S. cerevisiae, can provide the same function in E. coli. The screening for ampicillin resistance among blaS0 fusions provides a convenient method for the isolation of functional yeast and possibly higher eucaryotic signal sequences.
MeSH Terms
Biological Transport
Cell Membrane/metabolism
Cytoplasm/metabolism
DNA, Recombinant
Escherichia coli/metabolism
Fungal Proteins/analysis,genetics,metabolism
Protein Sorting Signals/analysis,genetics,metabolism
Saccharomyces cerevisiae/metabolism
beta-Lactamases/genetics,metabolism
Chemicals
DNA, Recombinant
Fungal Proteins
Protein Sorting Signals
beta-Lactamases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Roggenkamp R
Reipen G
Hollenberg C P
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