Nine amino acid residues at the NH2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli.

J. Ghrayeb, M. Inouye

Research output: Contribution to journalArticle

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Abstract

We have examined the structural requirements at the NH2-terminal region of the lipoprotein for its assembly in the outer membrane of Escherichia coli by constructing a hybrid protein consisting of an NH2-terminal portion of the prolipoprotein, consisting of the signal peptide and 9 amino acid residues of lipoprotein, and the entire beta-lactamase sequence. The results from this study indicate that the hybrid protein is modified with glyceride, processed in a globomycin-sensitive step, and localized in the outer membrane. The translocation of the hybrid protein across the cytoplasmic membrane occurs post-translationally and is inhibited by carbonyl cyanide m-chlorophenylhydrazone. Our results, therefore, indicate that the signal peptide and 9 amino acid residues of prolipoprotein are sufficient for its modification, processing, and localization in the outer membrane.

Original languageEnglish (US)
Pages (from-to)463-467
Number of pages5
JournalJournal of Biological Chemistry
Volume259
Issue number1
StatePublished - Jan 10 1984
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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