Structural basis of V-ATPase V_O region assembly by Vma12p, 21p, and 22p.

ABSTRACT: Vacuolar-type adenosine triphosphatases (V-ATPases) are rotary proton pumps that acidify specific intracellular compartments in almost all eukaryotic cells. These multi-subunit enzymes consist of a soluble catalytic V₁ region and a membrane-embedded proton-translocating V_O region. V_O is assembled in the endoplasmic reticulum (ER) membrane, and V₁ is assembled in the cytosol. However, V₁ binds V_O only after V_O is transported to the Golgi membrane, thereby preventing acidification of the ER. We isolated V_O complexes and subcomplexes from Saccharomyces cerevisiae bound to V-ATPase assembly factors Vma12p, Vma21p, and Vma22p. Electron cryomicroscopy shows how the Vma12-22p complex recruits subunits a

SUBMITTER: Wang H 

PROVIDER: S-EPMC9963935 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature