Award details

Structural and functional analysis of the specialised BRCT domain of E. coli DNA ligase

ReferenceC11893
Principal Investigator / Supervisor Dr Richard Bowater
Co-Investigators /
Co-Supervisors
Institution University of East Anglia
DepartmentBiological Sciences
Funding typeResearch
Value (£) 108,356
StatusCompleted
TypeResearch Grant
Start date 01/02/2000
End date 01/02/2002
Duration24 months

Abstract

BRCT domains are present in a range of DNA repair proteins and their mutation is linked to important human diseases, including breast cancer. Frequently, these motifs specify essential protein- protein contacts, which occur via unknown mechanisms. This project will characterise an unusual BRCT domain from E. coli DNA ligase. Mutagenesis studies will identify the role of specific residues within this motif. Full-length and fragments of DNA ligase will be purified and their ability to bind to DNA and other proteins will be analysed biochemically. Yeast two-hybrid and co- immunoprecipitation assays will characterise interactions occurring in vivo. The ease of genetic manipulations within E. coli is a major advantage for analysis of BRCT domains. In addition, these studies advance our knowledge of prokaryotic DNA ligases, a target for novel antibiotics.

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 X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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