کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2050819 | 1074182 | 2010 | 5 صفحه PDF | دانلود رایگان |
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.
Journal: FEBS Letters - Volume 580, Issue 8, 3 April 2006, Pages 2006–2010