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Molecular and biochemical analysis of the distinctive organelle-specific plant pyruvate dehydrogenase complexes

ReferenceP10229
Principal Investigator / Supervisor Professor John Lindsay
Co-Investigators /
Co-Supervisors
Professor Richard Cogdell
Institution University of Glasgow
DepartmentIBLS Division of Biochemistry & Molecula
Funding typeResearch
Value (£) 199,096
StatusCompleted
TypeResearch Grant
Start date 01/01/1999
End date 01/01/2003
Duration48 months

Abstract

a) purified chloroplastic E2, expressed as a GST fusion protein and its overexpressed N-terminal didomain will be employed i) as probes to examine the specificity, affinity and stoichiometry of E2 interactions with its companion E1/E3 components and ii) in 'pull-down' assays to detect candidate proteins such as antioxidant or other stress- related proteins which form physiologically relevant interactions with the complex; b) characterisation of plastidic E3 cDNA clones will be completed; c) the developmental regulation of mitochondrial and plastidic E3s will be monitored at transcriptional, translational and activity levels; d) characterisation of clones encoding the alpha- isoform of potato mitochondrial E3 will be performed as will structure-function analysis of the enzymatic properties and precise physiological roles of the 3 distinct E3 isoforms.

Summary

unavailable
Committee Closed Committee - Plant & Microbial Sciences (PMS)
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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