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Subunit Organization of the Stator Part of the F 0 Complex from Escherichia coli ATP Synthase

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Abstract

Membrane-bound ATP synthases (F1F0) catalyze the synthesis of ATP via a rotary catalyticmechanism utilizing the energy of an electrochemical ion gradient. The transmembrane potentialis supposed to propel rotation of a subunit c ring of F0 together with subunits γ and ∈ of F1,hereby forming the rotor part of the enzyme, whereas the remainder of the F1F0 complexfunctions as a stator for compensation of the torque generated during rotation. This reviewfocuses on our recent work on the stator part of the F0 complex, e.g., subunits a and b. Usingepitope insertion and antibody binding, subunit a was shown to comprise six transmembranehelixes with both the N- and C-terminus oriented toward the cytoplasm. By use of circulardichroism (CD) spectroscopy, the secondary structure of subunit b incorporated intoproteoliposomes was determined to be 80% α-helical together with 14% β turn conformation, providingflexibility to the second stalk. Reconstituted subunit b together with isolated ac subcomplexwas shown to be active in proton translocation and functional F1 binding revealing the nativeconformation of the polypeptide chain. Chemical crosslinking in everted membrane vesiclesled to the formation of subunit b homodimers around residues bQ37 to bL65, whereas bA32Ccould be crosslinked to subunit a, indicating a close proximity of subunits a and b near themembrane. Further evidence for the proposed direct interaction between subunits a and b wasobtained by purification of a stable ab 2 subcomplex via affinity chromatography using Histags fused to subunit a or b. This ab 2 subcomplex was shown to be active in proton translocationand F1 binding, when coreconstituted with subunit c. Consequences of crosslink formationand subunit interaction within the F1F0 complex are discussed.

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Authors and Affiliations

  1. Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, Universität Osnabrück, D-49069, Osnabrück, Germany

    Jörg-Christian Greie

  2. Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, Universität Osnabrück, D-49069, Osnabrück, Germany

    Gabriele Deckers-Hebestreit & Karlheinz Altendorf

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  1. Jörg-Christian Greie
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  2. Gabriele Deckers-Hebestreit
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  3. Karlheinz Altendorf
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Greie, JC., Deckers-Hebestreit, G. & Altendorf, K. Subunit Organization of the Stator Part of the F 0 Complex from Escherichia coli ATP Synthase . J Bioenerg Biomembr 32, 357–364 (2000). https://doi.org/10.1023/A:1005523902800

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