A dual role for phosphatidylglycerol in protein translocation across the Escherichia coli inner membrane

Ron Kusters, Eefjan Breukink, Andreas Gallusser, Andreas Kuhn, Ben De Kruijff

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    Abstract

    The involvement of phosphatidylglycerol in the SecA-independent translocation of M13 procoat in Escherichia coli was demonstrated. Processing of procoat to mature coat protein was retarded when the level of phosphatidylglycerol was reduced. In vitro translocation experiments using inner membrane vesicles isolated from a strain with inducible synthesis of phosphatidylglycerol, showed that translocation of procoat and of a SecA- dependent procoat analog was proportional to the content of phosphatidylglycerol. Moreover, introduction of phosphatidylglycerol by means of a lipid transfer method into phosphatidylglycerol-depleted inner membrane vesicles, efficiently restored procoat translocation. The phosphatidylglycerol dependence in both the SecA-dependent and -independent translocation pathway indicates that phosphatidylglycerol plays a dual role in translocation. We suggest that besides membrane binding of SecA this lipid has a direct interaction with the M13 procoat in translocation across the inner membrane.

    Original languageEnglish
    Pages (from-to)1560-1563
    Number of pages4
    JournalJournal of biological chemistry
    Volume269
    Issue number2
    Publication statusPublished - 14 Jan 1994

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    Phosphatidylglycerols
    Protein Transport
    Escherichia coli
    Membranes
    Proteins
    Lipids
    Capsid Proteins
    Processing

    Cite this

    Kusters, Ron ; Breukink, Eefjan ; Gallusser, Andreas ; Kuhn, Andreas ; De Kruijff, Ben. / A dual role for phosphatidylglycerol in protein translocation across the Escherichia coli inner membrane. In: Journal of biological chemistry. 1994 ; Vol. 269, No. 2. pp. 1560-1563.
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    abstract = "The involvement of phosphatidylglycerol in the SecA-independent translocation of M13 procoat in Escherichia coli was demonstrated. Processing of procoat to mature coat protein was retarded when the level of phosphatidylglycerol was reduced. In vitro translocation experiments using inner membrane vesicles isolated from a strain with inducible synthesis of phosphatidylglycerol, showed that translocation of procoat and of a SecA- dependent procoat analog was proportional to the content of phosphatidylglycerol. Moreover, introduction of phosphatidylglycerol by means of a lipid transfer method into phosphatidylglycerol-depleted inner membrane vesicles, efficiently restored procoat translocation. The phosphatidylglycerol dependence in both the SecA-dependent and -independent translocation pathway indicates that phosphatidylglycerol plays a dual role in translocation. We suggest that besides membrane binding of SecA this lipid has a direct interaction with the M13 procoat in translocation across the inner membrane.",
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    A dual role for phosphatidylglycerol in protein translocation across the Escherichia coli inner membrane. / Kusters, Ron; Breukink, Eefjan; Gallusser, Andreas; Kuhn, Andreas; De Kruijff, Ben.

    In: Journal of biological chemistry, Vol. 269, No. 2, 14.01.1994, p. 1560-1563.

    Research output: Contribution to journalArticleAcademicpeer-review

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    AU - Kusters, Ron

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