Award details

Membrane translocation of a toxin endonuclease

ReferenceB12974
Principal Investigator / Supervisor Professor Colin Kleanthous
Co-Investigators /
Co-Supervisors
Institution University of York
DepartmentBiology
Funding typeResearch
Value (£) 198,311
StatusCompleted
TypeResearch Grant
Start date 01/10/2000
End date 30/09/2003
Duration36 months

Abstract

The endonuclease domain from the bacterial toxin colicin E9 can translocate across membranes in the absence of energy or receptor proteins. Using bilayer experiments, unilamellar vesicles (in combination with a range of biophysical techniques) and the crystal structure of the DNase to design mutants we will: 1) Optimise the conditions for membrane translocation. 2) Investigate the properties of DNase channels. 3) Examine the effect of immunity protein binding on membrane translocations. 4) Address the link between DNase conformational stability and membrane translocation. 5) Define protein structural changes associated with membrane binding. 6) Investigate protein-membrane interactions and protein import into liposomes.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
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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