The plasmid pSW1 expresses the Bacteriocin Release Protein (BRP) upon induction, initiating release of periplasmic and cytoplasmic E. coli proteins into the culture medium.
BRP vectors are compatible with most of the commonly used expression vector systems and can be co-transformed with the vector producing the recombinant protein of interest. Induction of the BR-Protein with mitomycin C will cause an activation of phospholipase A in the outer E. coli membrane. This results in the formation of permeable zones in the cell membranes through which proteins are released into the medium. A moderate induction prevents lysis of producer cells, making the system suitable for large-scale protein production in a continuous culture. Since cloned proteins are no longer accumulated in the cytoplasm, issues with recombinant proteins lethality, preferential degradation, and inclusion body formation are avoided.
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