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| How does pmf drive the bacterial Tol assembly? | ||||||||||||||||||
The Tol assembly is a supramolecular complex in all Gram-negative bacteria which spans the periplasm and is composed of both membrane and soluble proteins. Composed of 5 core proteins, the assembly is required for virulence in pathogenic organisms such as Vibrio cholerae, Pseudomonas aeruginosa and Salmonella typhimurium. Coupled to the proton motive force (pmf) across the inner membrane, the Tol assembly is important for maintaining the stability of the outer membrane but in what capacity is not known. Protein-protein interactions play a crucial role in the functioning of the complex, with these associations influenced by the pmf. Through a combination of biochemical, biophysical and mutational approaches the aim of the project is to discover how pmf controls the interactions of the Tol assembly in E. coli, discoveries that may lead to a new generation of antimicrobial strategies aimed at inactivating the assembly in pathogens. Funding Notes This research project is one of a number of projects in the department. It is in competition for funding with the other projects. Usually the project which receives the best applicant will be awarded the funding. The funding is available to citizens of a number of European countries (including the UK). In most cases this will include all EU nationals. However full funding may not be available to all applicants. |
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Research Assessment Exercise (RAE) 2008 Results
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