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Molecular interactions during the unfolding membrane translocation and refolding of a cytotoxic protein
Reference
B08000
Principal Investigator / Supervisor
Professor Lynne Roberts
Co-Investigators /
Co-Supervisors
Professor Michael Lord
,
Professor Sheena Radford
Institution
University of Warwick
Department
Biological Sciences
Funding type
Research
Value (£)
148,665
Status
Completed
Type
Research Grant
Start date
13/11/1997
End date
31/03/2000
Duration
29 months
Abstract
Protein toxins such as ricin appear to enter the cytosol by translocating the endoplasmic reticulum (ER) membrane. The formation of a partially unfolded ricin A chain under conditions predicted to occur within the ER suggests that the protein unfolds to assume a form required for translocation-competence, refolding later in the presence of its ribosomal substrates to regain full activity (data from our preliminary studies). Using a combination of biophysical and biochemical approaches, we now propose to probe the interactions involved in the partial unfolding, membrane partitioning and refolding steps by using in vitro systems with purified components such as molecular chaperones, liposomes/membranes and ribosomes/subribosomal particles and rRNA.
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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