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CCT minichaperones as probes of the molecular basis of heterogenous CCT constitution

Reference	C09429
Principal Investigator / Supervisor	Dr Martin Carden
Co-Investigators / Co-Supervisors
Institution	University of Kent
Department	Sch of Biosciences
Funding type	Research
Value (£)	56,104
Status	Completed
Type	Research Grant
Start date	01/04/1998
End date	01/04/1999
Duration	12 months

Abstract

An explanation for the heterogenous constitution of the eukaryotic (CCT) chaperonin is required. We have generated some of the first evidence supporting the hypothesis that individual CCT subunits may perform different functions within cells and, moreover, not always as part of an oligomeric chaperonin particle. The proposed study will probe this further using a recently developed paradigmatic approach: (1) the apical (peptide- binding) domains of CCT subunits will be expressed as recombinant 'minichaperone' proteins; (2) their comparative substrate binding specificities and folding activities will be determined alongside purified CCT protein; (3) Antibodies inhibitory of these activities will be generated and characterised to identify and probe CCT subunit-specific functions and substrates. In addition to answering the important question of what each CCT subunit contributes to assisted protein folding in eukaryotes the study is also likely to generate several new projects with significance for understanding the basic cell and molecular biology of CCT and have important biotechnological applications.

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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