PMID:21900248
| Citation |
Pierson, HE, Uhlemann, EM and Dmitriev, OY (2011) Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation. J. Biol. Chem. 286:38583-91 |
|---|---|
| Abstract |
Subunit a is the main part of the membrane stator of the ATP synthase molecular turbine. Subunit c is the building block of the membrane rotor. We have generated two molecular fusions of a and c subunits with different orientations of the helical hairpin of subunit c. The a/c fusion protein with correct orientation of transmembrane helices was inserted into the membrane, and co-incorporated into the F(0) complex of ATP synthase with wild type subunit c. The fused c subunit was incorporated into the c-ring tethering the ATP synthase rotor to the stator. The a/c fusion with incorrect orientation of the c-helices required wild type subunit c for insertion into the membrane. In this case, the fused c subunit remained on the periphery of the c-ring and did not interfere with rotor movement. Wild type subunit a inserted into the membrane equally well with wild type subunit c and c-ring assembly mutants that remained monomeric in the membrane. These results show that interaction with monomeric subunit c triggers insertion of subunit a into the membrane, and initiates formation of the a-c complex, the ion-translocating module of the ATP synthase. Correct assembly of the ATP synthase incorporating topologically correct fusion of subunits a and c validates using this model protein for high resolution structural studies of the ATP synthase proton channel. |
| Links |
PubMed PMC3207401 Online version:10.1074/jbc.M111.294868 |
| Keywords |
Adenosine Triphosphatases/chemistry; Bacterial Proton-Translocating ATPases/chemistry; Biological Transport; Catalysis; Cell Membrane/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Molecular Conformation; Plasmids/metabolism; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Proton-Translocating ATPases/chemistry; Protons; Recombinant Fusion Proteins/chemistry |
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