OmpF-Lpp signal sequence mutants with varying charge hydrophobicity ratios provide evidence for a phosphatidylglycerol-signal sequence interaction during protein translocation across the Escherichia coli inner membrane

David A. Phoenix, R. Kusters, Chinami Hikita, Shoji Mizushima, Ben De Kruijff

    Research output: Contribution to journalArticleAcademicpeer-review

    50 Citations (Scopus)
    22 Downloads (Pure)

    Abstract

    Using inverted Escherichia coli inner membrane vesicles we have analyzed the phosphatidylglycerol dependence of translocation of an OmpF-Lpp fusion protein carrying a signal sequence with varying positive charge at the N terminus and a hydrophobic core of varying length. It is shown that there is a direct relationship between the phosphatidylglycerol requirement of translocation and the requirement within the translocation process for positive charges on the signal sequence. This provides further evidence that the negative head group of the lipid is required for functional interaction with the positively charged N terminus of the signal sequence.

    Original languageEnglish
    Pages (from-to)17069-17073
    Number of pages5
    JournalJournal of biological chemistry
    Volume268
    Issue number23
    Publication statusPublished - 1 Jan 1993

    Fingerprint Dive into the research topics of 'OmpF-Lpp signal sequence mutants with varying charge hydrophobicity ratios provide evidence for a phosphatidylglycerol-signal sequence interaction during protein translocation across the Escherichia coli inner membrane'. Together they form a unique fingerprint.

    Cite this