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J Biol Chem, Vol. 273, Issue 27, 17178-17185, July 3, 1998
From the Department of Biomolecular Chemistry, University of
Wisconsin Medical School, Madison, Wisconsin 53706
The multicopy subunit c of the
H+-transporting F1F0 ATP
synthase of Escherichia coli is thought to fold across the
membrane as a hairpin of two hydrophobic
Arrangement of the Multicopy H+-translocating Subunit
c in the Membrane Sector of the Escherichia coli
F1F0 ATP Synthase
-helices. The conserved
Asp61, centered in the second transmembrane helix, is
essential for H+ transport. In this study, we have made
sequential Cys substitutions across both transmembrane helices and used
disulfide cross-link formation to determine the oligomeric arrangement
of the c subunits. Cross-link formation between single Cys
substitutions in helix 1 provided initial limitations on how the
subunits could be arranged. Double Cys substitutions at positions
14/16, 16/18, and 21/23 in helix 1 and 70/72 in helix 2 led to the
formation of cross-linked multimers upon oxidation. Double Cys
substitutions in helix 1 and helix 2, at residues 14/72, 21/65, and
20/66, respectively, also formed cross-linked multimers. These results
indicate that at least 10 and probably 12 subunits c interact in a
front-to-back fashion to form a ring-like arrangement in
F0. Helix 1 packs at the interior and helix 2 at the
periphery of the ring. The model indicates that the Asp61
carboxylate is centered between the helical faces of adjacent subunit c
at the center of a four-helix bundle.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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