Assembly of the yeast vacuolar H+‐ATPase and ATP hydrolysis occurs in the absence of subunit c″
- 3 May 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (14) , 2981-2985
- https://doi.org/10.1016/j.febslet.2005.04.049
Abstract
The V-ATPases are ubiquitous enzymes of eukaryotes. They are involved in many cellular processes via their ability to pump protons across biological membranes. They are two domain enzymes comprising an ATP hydrolysing sector and a proton translocating sector. Both sectors are functionally coupled. The proton tanslocating sector, V0, is comprised of five polypeptides in an as yet undetermined stoichiometry. In V0 three homologous proteins, subunit c, c′ and c″ have previously been reported to be essential for assembly of the enzyme. However, we report that subunit c″ is not essential for assembly but is for functional coupling of the enzymeKeywords
This publication has 21 references indexed in Scilit:
- The First Putative Transmembrane Segment of Subunit c“ (Vma16p) of the Yeast V-ATPase Is Not Necessary for FunctionPublished by Elsevier ,2003
- Composition of the central stalk of the Na+‐pumping V‐ATPase from Caloramator fervidusEMBO Reports, 2002
- Evidence that there are two copies of subunit c″ in V0 complexes in the vacuolar H+-ATPaseBiochemical Journal, 2002
- Direct observation of the rotation of F1-ATPaseNature, 1997
- VMA11 and VMA16 Encode Second and Third Proteolipid Subunits of the Saccharomyces cerevisiae Vacuolar Membrane H+-ATPasePublished by Elsevier ,1997
- Helical structure and folding of subunit c of F1F0 ATP synthase: Proton NMR resonance assignments and NOE analysisBiochemistry, 1993
- Disposition and Orientation of Ductin (DCCD-Reactive Vacuolar H+-ATPase Subunit) in Mammalian Membrane ComplexesExperimental Cell Research, 1993
- Connexins and the vacuolar proteolipid-like 16-kDa protein are not directly associated with each other but may be components of similar or the same gap junctional complexesExperimental Cell Research, 1992
- H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of functionJournal of Bioenergetics and Biomembranes, 1992