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Volume 272, Number 27, Issue of July 4, 1997 pp. 16868-16872
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Reconstitution of FhuA, an Escherichia coli Outer Membrane Protein, into Liposomes
BINDING OF PHAGE T5 TO FhuA TRIGGERS THE TRANSFER OF DNA INTO THE PROTEOLIPOSOMES

(Received for publication, February 5, 1997, and in revised form, April 8, 1997)

From the Laboratoire des Biomembranes, URA CNRS 1116, Université Paris-Sud, Bât 430, F-91405 Orsay Cedex, France

The Escherichia coli outer membrane protein FhuA catalyzes the transport of ferrichrome and is the receptor of bacteriophage T5. Purified FhuA was reconstituted into liposomes. The size of the proteoliposomes and the distribution of the proteins in the vesicles were determined by freeze fracture electron microscopy. Unilamellar vesicles with a diameter larger than 200 nm were observed frequently. FhuA was symetrically oriented in the proteoliposomes. Reconstituted FhuA was functional as binding of phage T5 induced the release of phage DNA and its transfer inside the vesicles.

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