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- Publisher
- Springer Journals
- Copyright
- Copyright © 2003 by Plenum Publishing Corporation
- Subject
- Chemistry; Organic Chemistry; Bioorganic Chemistry; Biochemistry, general; Animal Biochemistry; Animal Anatomy / Morphology / Histology
- ISSN
- 0145-479X
- eISSN
- 1573-6881
- DOI
- 10.1023/A:1025772730586
- Publisher site
- See Article on Publisher Site
Abstract
The yeast V-ATPase belongs to a family of V-type ATPases present in all eucaryotic organisms. In Saccharomyces cerevisiae the V-ATPase is localized to the membrane of the vacuole as well as the Golgi complex and endosomes. The V-ATPase brings about the acidification of these organelles by the transport of protons coupled to the hydrolysis of ATP. In yeast, the V-ATPase is composed of 13 subunits consisting of a catalytic V1 domain of peripherally associated proteins and a proton-translocating V0 domain of integral membrane proteins. The regulatory subunit, Vma13p, was the first V-ATPase subunit to have its crystal structure determined. In addition to proteins forming the functional V-ATPase complex, three ER-localized proteins facilitate the assembly of the V0 subunits following their translation and insertion into the membrane of the ER. Homologues of the Vma21p assembly factor have been identified in many higher eukaryotes supporting a ubiquitous assembly pathway for this important enzyme complex.
Journal
Journal of Bioenergetics and Biomembranes – Springer Journals
Published: Oct 5, 2004