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.
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.
Plançon
L
L
Laboratoire des Biomembranes, URA CNRS 1116, Université Paris-Sud, Bât 430, F-91405 Orsay Cedex, France.
Chami
M
M
Letellier
L
L
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D003851:Deoxyribonucleases / Q000378:metabolism; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D005614:Freeze Fracturing; D018014:Gene Transfer Techniques; D008081:Liposomes / Q000378:metabolism*; D008274:Magnesium / Q000378:metabolism; D008854:Microscopy, Electron; D011510:Proteolipids / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D013604:T-Phages / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C050900:FhuA protein, E coli; D008081:Liposomes; D011510:Proteolipids; D011991:Receptors, Virus; C020485:proteoliposomes; D004247:DNA; D003851:Deoxyribonucleases; D008274:Magnesium