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Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy
Author(s) -
Zhang Zhenyu,
Inoue Takao,
Forgac Michael,
Wilkens Stephan
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.001
Subject(s) - protein subunit , electron microscope , v atpase , yeast , microbiology and biotechnology , chemistry , cryo electron microscopy , vacuole , atpase , biology , biophysics , biochemistry , enzyme , cytoplasm , physics , gene , optics
Vacuolar ATPases (V 1 V 0 ‐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.