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System-specific chaperones on the Tat protein transport pathway
Reference
BBS/B/07780
Principal Investigator / Supervisor
Professor Frank Sargent
Co-Investigators /
Co-Supervisors
Professor David Richardson
Institution
University of East Anglia
Department
Biological Sciences
Funding type
Research
Value (£)
207,582
Status
Completed
Type
Research Grant
Start date
01/06/2004
End date
31/01/2007
Duration
32 months
Abstract
The twin-arginine protein transport (Tat) system is a remarkable molecular machine dedicated to the translocation of fully folded proteins across energy-transducing membranes. Cofactor-containing Tat substrates such as trimethylamine N-oxide reductase acquire their cofactors prior to export and substrate proteins actually require to be folded before transport can proceed. Thus it is very likely that mechanisms exist to prevent wasteful export of immature Tat substrates or curb competition between immature and mature substrates for the transporter. Using the model prokaryote Escherichia coli and the TorD molecular chaperone system, we will define the proofreading activity on the Tat pathway at the molecular and cellular levels.
Summary
unavailable
Committee
Closed Committee - Plant & Microbial Sciences (PMS)
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
Associated awards:
BBS/B/07780/2 System-specific chaperones on the Tat protein transport pathway
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