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Mechanism & significance of disassembly by the Eukaryotic Chaperonin CCT (Chaperonin containing TCP-1)
Reference
BBS/B/13101
Principal Investigator / Supervisor
Dr Martin Carden
Co-Investigators /
Co-Supervisors
Institution
University of Kent
Department
Sch of Biosciences
Funding type
Research
Value (£)
310,768
Status
Completed
Type
Research Grant
Start date
01/04/2004
End date
31/03/2007
Duration
36 months
Abstract
CCT is required in folding specifically eukaryotic proteins. GroEL cannot replace this function but CCT mechanism is largely understood by comparison to this much better studied bacterial chaperonin. We repeatedly observe evidence for significant instability of holoCCT. This project will establish the mechanistic detail and functional significance of this ATP hydrolysis-dependent disassembly in three contexts; cells, semi-purified folding competent extracts, and highly purified holoCCT using actin as model client. Findings will provide a greater understanding of the functional and mechanistic differences between type I and type II (eukaryotic) chaperonins, especially within the neglected cellular context.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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