Close-up and genomic views of the yeast vacuolar H+-ATPase.
The yeast V-ATPase has emerged as an excellent model for other eukaryotic V-ATPases. In this review, recent biochemical and genomic studies of the yeast V-ATPase are described, with a focus on: 1) the role of V(1) subunit H in coupling ATP hydrolysis and proton pumping and 2) identification of the full set of yeast haploid deletion mutants that exhibit the pH and calcium-sensitive growth characteristic of loss of V-ATPase activity. The combination of "close-up" biochemical views of V-ATPase structure and mechanism and "geomic" views of its functional reach promises to provide new insights into the physiological of V-ATPases.
Kane
Patricia M
PM
Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 East Adams St., Syracuse, New York 13210, USA. kanepm@upstate.edu
D005656:Fungal Proteins / Q000235:genetics; D016681:Genome, Fungal; D009154:Mutation; D021122:Protein Subunits / Q000502:physiology; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D005656:Fungal Proteins; D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases