Structural requirement at the cleavage site for efficient processing of the lipoprotein secretory precursor of Escherichia coli

S. Inouye, G. Duffaud, M. Inouye

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

A phenotypically silent mutation in the signal peptide of the Escherichia coli outer membrane prolipoprotein was combined with other mutations in the mature lipoprotein structure. Under conditions where the individual mutations permit normal lipoprotein secretion, the prolipoprotein with both mutations was unable to be normally modified or processed. These results demonstrate that a given signal peptide is fully functional only if it is structurally compatible with the protein to be secreted. This structural compatibility between the signal peptide and the secretory protein is considered to be dependent on the secondary structure formed at or near the signal peptide cleavage site.

Original languageEnglish (US)
Pages (from-to)10970-10975
Number of pages6
JournalJournal of Biological Chemistry
Volume261
Issue number24
StatePublished - 1986

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Structural requirement at the cleavage site for efficient processing of the lipoprotein secretory precursor of Escherichia coli'. Together they form a unique fingerprint.

Cite this