Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits.

  title={Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits.},
  author={Isabel Arnold and Kathy Pfeiffer and Walter Neupert and Rosemary A. Stuart and Hermann Sch{\"a}gger},
  journal={The EMBO journal},
  volume={17 24},
Using the technique of blue native gel electrophoresis, the oligomeric state of the yeast mitochondrial F1F0-ATP synthase was analysed. Solubilization of mitochondrial membranes with low detergent to protein ratios led to the identification of the dimeric state of the ATP synthase. Analysis of the subunit composition of the dimer, in comparison with the monomer, revealed the presence of three additional small proteins. These dimer-specific subunits of the ATP synthase were identified as the… CONTINUE READING
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  • M. Prescott, G. Boyle, A Lourbakous, P. Nagely, R. J. Devenish
  • Yeast
  • 1997
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  • J. M. Herrmann, H. Fölsch, W. Neupert, R. A. Stuart
  • In Celis,D.E. (ed.), Cell Biology: A Laboratory…
  • 1994
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Yeast mitochondrial F 1 F 0 - ATPase : the novel subunit e is identical to Tim 11

  • M. F. Bauer, M. Brunner, W. Neupert
  • FEBS Lett
  • 1997

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