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System-specific chaperones on the Tat protein transport pathway

ReferenceBBS/B/07780/2
Principal Investigator / Supervisor Professor Frank Sargent
Co-Investigators /
Co-Supervisors
Professor David Richardson
Institution University of Dundee
DepartmentSchool of Life Sciences
Funding typeResearch
Value (£) 31,970
StatusCompleted
TypeResearch Grant
Start date 01/11/2007
End date 30/06/2008
Duration8 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 TopicsMicrobiology
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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