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Cochaperone facilitated protein folding in vitro and in vivo
Reference
B13401
Principal Investigator / Supervisor
Professor Michael Cheetham
Co-Investigators /
Co-Supervisors
Dr James Chapple
Institution
University College London
Department
Institute of Ophthalmology
Funding type
Research
Value (£)
227,988
Status
Completed
Type
Research Grant
Start date
01/04/2000
End date
01/04/2003
Duration
36 months
Abstract
The DnaJ family of cochaperones is the largest and most diverse chaperone family, with over 40 members currently described in mammals. We have identified a new DnaJ subfamily characterised by the conservation of the motif ENGQERVEVEEDG. This subfamily is also characterised by specialised patterns of expression that may be related to cell specific function or tissue development (e.g. Mrj and placenta). We have demonstrated that the prototypical member of this family, HSJ1, can act as a chaperone in vitro and in vivo, with striking differences in function between the two alternatively spliced isoforms. This proposal aims to define the molecular basis of the chaperone action of this chaperone subfamily and the different functions of the two isoforms by correlating in vitro and in vivo studies of protein structure and function.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
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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