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

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

53 Citations (Scopus)
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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
Externally publishedYes

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