Export and secretion of overproduced OmpA-β-lactamase in Escherichia coli

Jean Michel Bolla, Claude Lazdunski, Masayori Inouye, Jean Marie Pagès

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


The export of β-lactamase to the periplasm of Escherichia coli can be directed by the OmpA signal peptide in the secretion cloning vector pIN-III. The overproduction of the hybrid precursor specifically induces a delay in the onset of processing of newly synthesized polypeptide chains. However, when the processing starts, no alteration in the rate of cleavage itself is observed. Our results suggest that the temporal mode of processing (which reflects translocation) does not depend on the nature of the signal peptide but rather depends on the nature of the polypeptide chain exported.

Original languageEnglish (US)
Pages (from-to)213-218
Number of pages6
JournalFEBS Letters
Issue number1
StatePublished - Nov 16 1987

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


  • Hybrid protein
  • Periplasmic protein
  • Protein export
  • Protein processing
  • Signal peptide


Dive into the research topics of 'Export and secretion of overproduced OmpA-β-lactamase in Escherichia coli'. Together they form a unique fingerprint.

Cite this