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.
Department of Biochemistry, University of California, Riverside, Riverside, CA 92521, USA.
Zhenyu
Z
Zhang
Takao
T
Inoue
Michael
M
Forgac
Stephan
S
Wilkens
D000911:Antibodies, Monoclonal; D016253:Microscopy, Immunoelectron; D008958:Models, Molecular; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism*; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*
D000911:Antibodies, Monoclonal; D021122:Protein Subunits; D029701:Saccharomyces cerevisiae Proteins; C447616:VMA5 protein, S cerevisiae; D025262:Vacuolar Proton-Translocating ATPases