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Figure 2 | Microbial Cell Factories

Figure 2

From: Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli

Figure 2

Flow-chart summarizing the different possibilities for producing disulfide-dependent proteins in bacteria. Expression is optimized and protein folding directed either in the cytoplasm or in the periplasm. Once folded in the cytoplasm, proteins can accumulate in the same cell compartment, or be exported to the periplasm by the Tat-pathway, or be secreted to the medium by the type I secretion system. Unfolded proteins can be translocated post-translationaly (Sec) or co-translationaly (SPR) into the periplasm and accumulate there, leak to the medium, or be exposed on the outer membrane. Precipitated proteins can be recovered into native structure by means of oxidative refolding.

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