Resolution of subunit interactions and cytoplasmic subcomplexes of the yeast vacuolar proton-translocating ATPase.

@article{Tomashek1996ResolutionOS,
  title={Resolution of subunit interactions and cytoplasmic subcomplexes of the yeast vacuolar proton-translocating ATPase.},
  author={John J. Tomashek and Justin L. Sonnenburg and J M Artimovich and Daniel J Klionsky},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 17},
  pages={10397-404}
}
The vacuolar proton-translocating ATPase is the principal energization mechanism that enables the yeast vacuole to perform most of its physiological functions. We have undertaken an examination of subunit-subunit interactions and assembly states of this enzyme. Yeast two-hybrid data indicate that Vma1p and Vma2p interact with each other and that Vma4p interacts with itself. Three-hybrid data indicate that the Vma4p self-interaction is stabilized by both Vma1p and Vma2p. Native gel… CONTINUE READING

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