Expression and secretion of proteins in E. coli

Ophry Pines*, Masayori Inouye

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

47 Scopus citations

Abstract

This review outlines approaches to the cloning and expression of proteins in Escherichia coli. The expression vectors described here (pIN-III derivatives) utilize the strong lipoprotein promoter, which is controlled by the lac-UV5 promoter-operator. These vectors provide the means for targeting a protein to any of the four subcellular compartments of the bacterial cell: cytoplasm, cytoplasmic membrane, periplasm, and outer membrane. Of particular importance is that secretion of proteins into the E. coli periplasm (using the OmpA signal peptide) is applicable for the production of both prokaryotic and eukaryotic proteins thereby enhancing protein activity and stability.

Original languageAmerican English
Pages (from-to)25-34
Number of pages10
JournalMolecular Biotechnology
Volume12
Issue number1
DOIs
StatePublished - 1999

Keywords

  • E. coli
  • Eukaryote
  • Expression vectors
  • OmpA
  • Prokaryote
  • Secretion
  • pIN-III

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