Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus

The FEBS Journal
Denys PogoryelovThomas Meier

Abstract

The interaction between the c(11)ring and the gammaepsilon complex, forming the rotor of the Ilyobacter tartaricus ATP synthase, was probed by surface plasmon resonance spectroscopy and in vitro reconstitution analysis. The results provide, for the first time, a direct and quantitative assessment of the stability of the rotor. The data indicated very tight binding between the c(11)ring and the gammaepsilon complex, with an apparent K(d) value of approximately 7.4nm. The rotor assembly was primarily dependent on the interaction of the cring with the gammasubunit, and binding of the cring to the free epsilon subunit was not observed. Mutagenesis of selected conserved amino acid residues of all three rotor components (cR45, cQ46, gammaE204, gammaF203 and epsilonH38) severely affected rotor assembly. The interaction kinetics between the gammaepsilon complex and c(11)ring mutants suggested that the assembly of the c(11)gammaepsiloncomplex was governed by interactions of low and high affinity. Low-affinity binding was observed between the polar loops of the cring subunits and the bottom part of the gamma subunit. High-affinity interactions, involving the two residues gammaE204 and epsilonH38, stabilized the holo-c(11)gammaepsilon com...Continue Reading

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Citations

Sep 29, 2009·Nature Structural & Molecular Biology·Denys PogoryelovThomas Meier
May 26, 2012·Proceedings of the National Academy of Sciences of the United States of America·Denys PogoryelovThomas Meier
Jul 29, 2009·The Journal of Biological Chemistry·Nelli MnatsakanyanJoachim Weber
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