Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy.

Abstract:

: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_name

FEBS Lett

journal_title

FEBS letters

authors

Zhang Z,Inoue T,Forgac M,Wilkens S

doi

10.1016/j.febslet.2006.03.001

keywords:

subject

Has Abstract

pub_date

2006-04-03 00:00:00

pages

2006-10

issue

8

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00290-0

journal_volume

580

pub_type

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