System-specific chaperones on the Tat protein transport pathway
Lead Research Organisation:
University of Dundee
Department Name: School of Life Sciences
Abstract
Abstracts are not currently available in GtR for all funded research. This is normally because the abstract was not required at the time of proposal submission, but may be because it included sensitive information such as personal details.
Technical Summary
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.
Organisations
Publications
Buchanan G
(2008)
Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.
in FEBS letters
Guymer D
(2010)
Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping.
in The FEBS journal
Guymer D
(2009)
A genetic analysis of in vivo selenate reduction by Salmonella enterica serovar Typhimurium LT2 and Escherichia coli K12.
in Archives of microbiology
Ize B
(2009)
Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains.
in Microbiology (Reading, England)
Maillard J
(2007)
Structural diversity in twin-arginine signal peptide-binding proteins.
in Proceedings of the National Academy of Sciences of the United States of America
Martinez-Espinosa RM
(2007)
Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases.
in FEMS microbiology letters
Sargent F
(2007)
The twin-arginine transport system: moving folded proteins across membranes.
in Biochemical Society transactions
Description | Very influencial project in the field. First NMR structures of a signal peptide binding protein were described, together with prize-winning papers (EURO 10,000 for a FEBS Letter of The Year) on protein-protein interactions. This grant helped to shape the field in terms of new knowledge on signal peptide recognition systems. |
Exploitation Route | Probably not in commerical terms, but protein-protein interactions govern biological systems so the scientific community will be enriched by this extra knowledge. It is possible that the systems here could be adapted to form a synthetic interaction system that could enhance or invent new biological activities. The University has an effective Research and Innovation Services Team that will be consulted with as appropriate. |
Sectors | Chemicals,Creative Economy,Education |
Description | Magnificent Microbes 2010 |
Form Of Engagement Activity | Participation in an open day or visit at my research institution |
Part Of Official Scheme? | No |
Geographic Reach | Regional |
Primary Audience | Public/other audiences |
Results and Impact | Interactive stalls and activities. Pupils and public were asked to complete questionairres after the event - teh feedback was positive. |
Year(s) Of Engagement Activity | 2010 |