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Cochaperone facilitated protein folding in vitro and in vivo

ReferenceB13401
Principal Investigator / Supervisor Professor Michael Cheetham
Co-Investigators /
Co-Supervisors
Dr James Chapple
Institution University College London
DepartmentInstitute of Ophthalmology
Funding typeResearch
Value (£) 227,988
StatusCompleted
TypeResearch Grant
Start date 01/04/2000
End date 01/04/2003
Duration36 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 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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