Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy.
Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy.
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通过免疫电子显微镜定位酵母液泡 ATP 酶中的亚基 C (Vma5p)。
DOI：
10.1016/j.febslet.2006.03.001
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发表时间：
2006
期刊：
影响因子：
3.5
通讯作者：
Wilkens,Stephan
中科院分区：
文献类型：
--
作者：
Zhang,Zhenyu;Inoue,Takao;Forgac,Michael;Wilkens,Stephan
极性ATP酶（V1 V0-ATP酶）在质子跨亚细胞区室的脂质膜转运中起作用。我们已经使用抗体标记和电子显微镜确定的位置，亚基C的液泡ATP酶从酵母。数据显示，亚基C结合在ATP酶和质子通道的界面处，与先前鉴定为亚基H的另一种茎密度相反[Wilkens S.，井上T.，和Forgac M.（2004）液泡ATP酶的三维结构-通过差异成像和化学交联定位H亚基。J. Biol. Chem. 279，41942-41949]。液泡ATP酶茎域的图片正在出现，其中亚基C和H被定位在可逆的酶解离和活性沉默中发挥作用。
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.