Assembly and Regulation of the Yeast Vacuolar H+-ATPase

• DOI: 10.1242/jeb.203.1.81
• Publication Date: 2021-04-25T05:36:08Z
• Authors: Patricia M. Kane; Karlett J. Parra
• Keywords: V-ATPase

ABSTRACT The yeast vacuolar H+ -ATPase (V-ATPase) consists of a complex peripheral subunits containing the ATP binding sites, termed V1 sector, attached to membrane proton pore, Vo sector. Interaction between and sectors is essential for ATP-driven transport, this interaction manipulated in vivo as means regulating V-ATPase activity. When (Saccharomyces cerevisiae) cells are deprived glucose little 5 min, up 75 % assembled complexes disassembled into cytoplasmic membrane-bound sectors. Remarkably, disassembly completely reversible. Restoration growth medium results quantitative reassembly even absence any new protein synthesis. Cells also appear regulate extent assembly on long-term basis. Yeast grown extended periods poor carbon source contain high proportion free sectors, these remain poised when conditions improve. Parallel experiments Manduca sexta suggest that reversible may be general regulatory mechanism V-ATPases. These imply V-ATPases surprisingly dynamic structures, their unique ‘regulated instability’ raises number interesting physiological structural questions. How extracellular such communicated present intracellular membranes? major changes generated how ‘silenced’ prevent unproductive hydrolysis by dissociated enzyme? We addressing questions using combination genetic biochemical approaches.