In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT.
The Escherichia coli outer membrane protease OmpT (protease VII) has been shown to degrade several proteins in vitro, but its function in vivo is uncertain. We demonstrate that OmpT participates in the degradation of a fusion protein secreted into the periplasmic space. A strain with mutations in degP (K.L. Strauch and J. Beckwith, Proc. Natl. Acad. Sci. USA 85:1576-1580, 1988) and ompT exhibits a cumulative decrease in protein degradation and should be useful for the expression of proteolytically sensitive secreted proteins.
Department of Chemical Engineering, University of Texas, Austin 78712.
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Baneyx
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Georgiou
D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D005798:Genes, Bacterial; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000502:physiology*; D013205:Staphylococcal Protein A / Q000378:metabolism*; D001618:beta-Lactamases / Q000378:metabolism*
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D012697:Serine Endopeptidases; C057840:omptin outer membrane protease; D001618:beta-Lactamases