Bacterial beta-lactamase is efficiently secreted in Saccharomyces cerevisiae under control of the invertase signal sequence.
The enzyme beta-lactamase, a secretory protein that is located in the Escherichia coli periplasmic space, can be highly expressed in Saccharomyces cerevisiae. Although the protein can cross eukaryotic membranes, it is only inefficiently secreted by yeast. To determine whether the lack of secretion in yeast is due to the nature of the bacterial signal sequence, it was replaced with the signal peptide of yeast invertase. The presence of the invertase signal peptide led to beta-lactamase secretion of up to 75%. The results indicate that the bacterial signal peptide is not functional in yeast, although cleavage can take place at the authentic processing site. The mature enzyme does not interfere with the yeast secretion pathway.
Bielefeld
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M
Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Federal Republic of Germany.
Hollenberg
C P
CP
D000595:Amino Acid Sequence; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D010957:Plasmids; D021382:Protein Sorting Signals / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D043324:beta-Fructofuranosidase; D001618:beta-Lactamases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase; D001618:beta-Lactamases