Proteomics

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Investigation of the effects on the proteome composition of Escherichia coli producing a recombinant protein in the periplasm under non-optimized and optimized conditions


ABSTRACT: Recombinant proteins containing disulfide bonds, like antibody fragments, are usually produced in the periplasm of E. coli, because in this compartment of the E. coli cell the formation of disulfide bonds is catalyzed. A recombinant protein is targeted to the periplasm with the help of an N-terminally fused signal sequence, which is clipped off from the recombinant protein upon translocation across the cytoplasmic membrane. The single-chain variable antibody fragment BL1 N-terminally fused to the DsbA signal sequence was produced in the E. coli Lemo21(DE3) recombinant protein production strain at conditions non-optimal (0 µM L-rhamnose) and optimal (500 µM L-rhamnose) for the production of the scFv BL1 in the periplasm. Lemo21(DE3) cells not producing a recombinant protein were used as a reference.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Escherichia Coli

SUBMITTER: Jimmy Ytterberg  

LAB HEAD: Roman A. Zubarev

PROVIDER: PXD008777 | Pride | 2019-11-12

REPOSITORIES: Pride

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Publications

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

Baumgarten Thomas T   Ytterberg A Jimmy AJ   Zubarev Roman A RA   de Gier Jan-Willem JW  

Applied and environmental microbiology 20180531 12


In <i>Escherichia coli</i>, 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 recomb  ...[more]

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