High-Level Periplasmic Expression in Escherichia coliUsing a Eukaryotic Signal Peptide: Importance of Codon Usage at the 5′ End of the Coding Sequence

Autor:	Humphreys, David P., Sehdev, Mukesh, Chapman, Andrew P., Ganesh, Ravindra, Smith, Bryan J., King, Lloyd M., Glover, David J., Reeks, Dominic G., Stephens, Paul E.
Zdroj:	Protein Expression and Purification; November 2000, Vol. 20 Issue: 2 p252-264, 13p
Abstrakt:	We investigated the ability of signal peptides of eukaryotic origin (human, mouse, and yeast) to efficiently direct model proteins to the Escherichia coliperiplasm. These were compared against a well-characterized prokaryotic signal peptide—OmpA. Surprisingly, eukaryotic signal peptides can work very efficiently in E. coli,but require optimization of codon usage by codon-based mutagenesis of the signal peptide coding region. Analysis of the 5′ of periplasmic and cytoplasmic E. coligenes shows some codon usage differences.
Databáze:	Supplemental Index
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