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The interaction of DNA gyrase with FdhE a protein involved in the assembly of the formate dehydrogenase complex

Reference9810615
Principal Investigator / Supervisor Professor Anthony Maxwell
Co-Investigators /
Co-Supervisors
Institution John Innes Centre
DepartmentBiological Chemistry
Funding typeResearch
Value (£) 138,336
StatusCompleted
TypeResearch Grant
Start date 01/03/1999
End date 14/07/2002
Duration40 months

Abstract

DNA gyrase is a type II topoisomerase from bacteria which controls the level of DNA supercoiling. Using affinity columns we have found evidence for specific interaction between the gyrase A subunit and FdhE, a protein involved in the assembly of the formate dehydrogenase complex in E. coli. Experiments in vitro show that TdhE can inhibit gyrase-catalysed DNA supercoiling and DNA binding. We have now made a fusion construct which expresses FdhE and plan to investigate its potential role in the regulation and control of the physiology and enzymology of DNA gyrase.

Summary

unavailable
Committee Closed Committee - Biochemistry & Cell Biology (BCB)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative ROPA 1998 (ROPA1998) [1998]
Funding SchemeX – not Funded via a specific Funding Scheme
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