Award details

Structure function and mechanism of archaeal uracil sensors

Reference	BBS/B/05060
Principal Investigator / Supervisor	Professor Bernard Connolly
Co-Investigators / Co-Supervisors	Dr Richard Lewis
Institution	Newcastle University
Department	Inst for Cell and Molecular Biosciences
Funding type	Research
Value (£)	184,758
Status	Completed
Type	Research Grant
Start date	01/07/2004
End date	30/06/2007
Duration	36 months

Abstract

Uracil is detrimental to genome function and all organisms contain enzymes to reduce its presence in DNA. Many archaea live at elevated temperatures, conditions that promote the conversion of G:C base-pairs to G:U mis-pairs and uracil sensors in archaea show unusual features which include: 1) unique ability of DNA polymerase to stall replication in response to template-strand uracil; 2) a novel protein-protein interaction between the polymerase and uracil-DNA-glycosylase (the enzyme which initiaties uracil repair by glycosidic bond cleavage). To fully understand uracil sensing in archaea, a biochemical and structural analysis of the polymerase and the UDG, concentrating on the polymerase-UDG interaction, will be carried out. In addition, the enzymes required to complete uracil repair will be isolated and characterised, allowing elucidation of key protein-protein interactions in the repair pathway.

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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