Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy.
Vacuolar ATPases (V1V0 -ATPases) function in proton translocation across lipid membranes of subcellular compartments. We have used antibody labeling and electron microscopy to define the position of subunit C in the vacuolar ATPase from yeast. The data show that subunit C is binding at the interface of the ATPase and proton channel, opposite from another stalk density previously identified as subunit H [Wilkens S., Inoue T., and Forgac M. (2004) Three-dimensional structure of the vacuolar ATPase - Localization of subunit H by difference imaging and chemical cross-linking. J. Biol. Chem. 279, 41942-41949]. A picture of the vacuolar ATPase stalk domain is emerging in which subunits C and H are positioned to play a role in reversible enzyme dissociation and activity silencing.[1]References
- Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy. Zhang, Z., Inoue, T., Forgac, M., Wilkens, S. FEBS Lett. (2006) [Pubmed]
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