Optimizing Recombinant Protein Production in the Escherichia coli Periplasm Alleviates Stress.

ABSTRACT: In Escherichia coli, many recombinant proteins are produced in the periplasm. To direct these proteins to this compartment, they are equipped with an N-terminal signal sequence so that they can traverse the cytoplasmic membrane via the protein-conducting Sec translocon. Recently, using the single-chain variable antibody fragment BL1, we have shown that harmonizing the target gene expression intensity with the Sec translocon capacity can be used to improve the production yields of a recombinant protein in the periplasm. Here, we have studied the consequences of improving the production of BL1 in the periplasm by using a proteomics approach. When the target gene expression intensity is not harmonized with the Sec translocon capacity, the impaired translocation of secretory proteins, p

SUBMITTER: Baumgarten T 

PROVIDER: S-EPMC5981079 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature