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Energy coupling and the basis of specificity of Escherichia coli topoisomerase IV
Reference
C06672
Principal Investigator / Supervisor
Dr Andrew Bates
Co-Investigators /
Co-Supervisors
Institution
University of Liverpool
Department
Sch of Biological Sciences
Funding type
Research
Value (£)
155,201
Status
Completed
Type
Research Grant
Start date
01/03/1997
End date
01/03/2000
Duration
36 months
Abstract
In recent years, topoisomerase IV, a new bacterial type II topoisomerase and antibacterial drug target has been identified, which is specifically involved in the ATP-dependent decatenation (unlinking) of daughter chromosomes. It is proposed to investigate the detailed biochemistry of E. coli topo IV, with a view to the elucidation of the basis of the selective coupling of ATP hydrolysis to the decatenation reaction, using assays of ATPase activity, ADPNP-dependent reactions and quinolone drug inhibition, with DNA substrates designed to reveal relaxation or decatenation activity. The structural basis of the enzyme's specificity will be addressed by characterisation of mutant and engineered forms of the enzyme.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
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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