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Structure and mechanism of the twin-arginine translocation (Tat) protein transporter

Reference	BBS/B/12091
Principal Investigator / Supervisor	Professor Colin Robinson
Co-Investigators / Co-Supervisors	Professor Corinne Smith
Institution	University of Warwick
Department	Biological Sciences
Funding type	Research
Value (£)	198,553
Status	Completed
Type	Research Grant
Start date	05/07/2004
End date	04/04/2008
Duration	45 months

Abstract

The Tat system catalyses the transport of fully-folded proteins across bacterial and plany thylakoid membranes but the structure and unique translocation mechanism of this system are very poorly understood. We have generated GFP fusions to all 3 primary Tat subunits and shown them to be active and correctly assembled. We propose to use these fusion proteins to (i) unravel the subunit interactions within and between Tat complexes using fluorescence resonance energy transfer measurements, (ii), understand the structure of TatABC using the GFP domains as markers in single particle electron microscopy studies and (iii) understand how the TatABC complex assembles from smaller units.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	Microbiology, Structural Biology
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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