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The molecular mechanism of T4 phage activated proteolytic cleavage of Escherichia coli translation elongation factor Tu
Reference
B07954
Principal Investigator / Supervisor
Professor Colin Kleanthous
Co-Investigators /
Co-Supervisors
Institution
University of East Anglia
Department
Biological Sciences
Funding type
Research
Value (£)
144,943
Status
Completed
Type
Research Grant
Start date
13/10/1997
End date
13/10/2000
Duration
36 months
Abstract
This proposal aims to dissect at the molecular level a defence mechanism that is activated in E. coli following infection by bacteriophage T4. A region of the T4 coat (the gol peptide) activates the Lit protease which cleaves EF-Tu leading to inhibition of translation. Three areas will be investigated: 1) The structure and mechanism of the Lit protease. 2) Mutagenesis of EF-Tu will probe the specificity of the cleavage reaction. The effects of nucleotide exchange and the cleavage of other GTP-binding proteins such as ras will also be analysed. 3) NMR will be used to determine the solution structure of the 29 residue gol peptide, which is sufficient to activate Lit. Spectroscopy and cross-linking will also be used to investigate the complexation of the gol peptide with either Lit or EF-Tu. The structure and activation properties of 'mutant' synthetic gol peptides will also be analysed.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
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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