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The membrane associated domain of the vacuolar H+-ATPase: assembly structure and function

ReferenceC10854
Principal Investigator / Supervisor Professor John B C Findlay
Co-Investigators /
Co-Supervisors
Institution University of Leeds
DepartmentInst of Molecular & Cellular Biology
Funding typeResearch
Value (£) 212,636
StatusCompleted
TypeResearch Grant
Start date 01/04/1999
End date 28/02/2003
Duration47 months

Abstract

The project will investigate the assembly, structure and function of the vacuolar H+-ATPase, and essential molecular complex of virtually all eukaryotic cells. These acid pumps have bipartite structure, with a soluble catalytic sector connected structurally and mechanistically to a membrane-bound proton translocating sector via stalk subunits. The study will focus on this intramembranous Vo sector and adjacent stalk subunits and will employ techniques in protein expression mutagenesis, chemical cross-linking and labelling, and functional analysis to elucidate the organisation, role and structure of subunits within these sectors. A major aim of the study will be to map the changes in key functional interactions which occur during the catalytic cycle of the pump. The site of binding of natural inhibitors, and the mechanism underlying their action, will also be determined.

Summary

unavailable
Committee Closed Committee - Biochemistry & Cell Biology (BCB)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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