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Protein binding at DNA ends: determining the specificity of multiple DNA binding sites within E. coli DNA ligase

ReferenceB16634
Principal Investigator / Supervisor Dr Richard Bowater
Co-Investigators /
Co-Supervisors
Professor Andrew Hemmings
Institution University of East Anglia
DepartmentBiological Sciences
Funding typeResearch
Value (£) 157,864
StatusCompleted
TypeResearch Grant
Start date 13/05/2002
End date 12/06/2004
Duration25 months

Abstract

DNA ligases join breaks in the backbone of DNA. In a current BBSRC-funded study, we have demonstrated that the C-terminal BRCT domain of E. coli DNA ligase binds DNA. Building on this intriguing observation, we aim to further our biochemical and mutagenesis analysis of the E. coli DNA ligase. We now propose a programme of crystallographic and biophysical studies in combination with mutational analyses that will be used to determine the structural basis for the macromolecular interaction between DNA and domains within the E. coli DNA ligase. These important studies will delineate the DNA-binding function of the BRCT domain in the eubacterial enzyme, which may be relevant to its role in a wide range of DNA repair proteins.

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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