Stoichiometry of the Peripheral Stalk Subunits E and G of Yeast V1-ATPase Determined by Mass Spectrometry*

@article{Kitagawa2008StoichiometryOT,
  title={Stoichiometry of the Peripheral Stalk Subunits E and G of Yeast V1-ATPase Determined by Mass Spectrometry*},
  author={Norton Kitagawa and Hortense Mazon and Albert J. R. Heck and Stephan Wilkens},
  journal={Journal of Biological Chemistry},
  year={2008},
  volume={283},
  pages={3329 - 3337}
}
The stoichiometry of yeast V1-ATPase peripheral stalk subunits E and G was determined by two independent approaches using mass spectrometry (MS). First, the subunit ratio was inferred from measuring the molecular mass of the intact V1-ATPase complex and each of the individual protein components, using native electrospray ionization-MS. The major observed intact complex had a mass of 593,600 Da, with minor components displaying masses of 553,550 and 428,300 Da, respectively. Second, defined… 
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A structural model of the A-ATPase peripheral stalk is proposed, which finds that the isolated C-terminal domain of the E subunit exists as a dimer in solution, consistent with a recent crystal structure of the related Pyrococcus horikoshii A- ATPase E subunits.
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It is proposed that upon disassembly, the H subunit undergoes a conformational change that inhibits V1-ATPase activity and precludes V0 interactions.
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