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J. Biol. Chem., Vol. 269, Issue 4, 2562-2567, Jan, 1994
D Fraga, J Hermolin and RH Fillingame
A mutant of ATP synthase subunit c was isolated in which the essential
aspartate was exchanged from position 61 on transmembrane helix-2 to
position 24 on transmembrane helix-1 (Miller, M. J., Oldenburg, M., and
Fillingame, R. H. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 4900- 4904).
The H+ transporting ATP synthase function of the Ala24--
>Asp/Asp61-->Gly mutant is not optimal, and cells grow more slowly
than wild type. Twenty-three third-site suppressor mutants with optimized
function were isolated in this study. Ten of the optimizing mutations were
located to helix-2 of subunit c, and seven of these fell in residues Phe53,
Met57, and Met65. The side chains of these three residues are proposed to
form a hydrophobic surface on transmembrane helix-2, which participates in
the presentation or occlusion of the essential aspartate carboxyl group
during proton translocation. The other 13 optimizing mutations were located
to subunit a, and 10 of these fell in residues Ala217, Ile221, and Leu224.
These three residues are proposed to lie on one face of a transmembrane
alpha-helix that includes the essential Arg210 residue. This helix is
proposed to interact with the transmembrane bihelical unit of subunit c
during protonation and deprotonation of the essential Asp24 in the mutant
or Asp61 in wild type.
Transmembrane helix-helix interactions in F0 suggested by suppressor mutations to Ala24-->Asp/Asp61-->Gly mutant of ATP synthase subunit
Department of Biomolecular Chemistry, University of Wisconsin Medical School, Madison 53706.
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