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(Received for publication, October 11, 1996, and in revised form, November 19, 1996)
From the Biozentrum, University of Basel,
CH-4056 Basel, Switzerland
An in vitro assay of iron-ferrichrome
translocation across the FhuA protein of outer membranes from
Escherichia coli has been devised. Upon reconstitution into
large lipid vesicles, bacteriophage T5 binds to this polyvalent
receptor, triggering a conformational change that resulted in channel
opening. This facilitates the translocation of an
iron(III)-siderophore, without the complexities involved in the
in vivo process. Efflux of
55Fe(III)-ferrichrome across FhuA channels was determined
quantitatively by monitoring the release of trapped radioactivity. The
assay is rapid, reliable, and specific, because other bacteriophages, such as
Volume 272, Number 3,
Issue of January 17, 1997
pp. 1448-1451
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
FhuA-MEDIATED FERRICHROME EFFLUX FROM LIPID VESICLES TRIGGERED
BY PHAGE T5
80, fail to trigger channel opening of the FhuA
receptor.
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