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Structure-specific interaction of HMG1 with DNA and chromatin
Reference
B12904
Principal Investigator / Supervisor
Professor Dame Jean Olwen Thomas
Co-Investigators /
Co-Supervisors
Institution
University of Cambridge
Department
Biochemistry
Funding type
Research
Value (£)
217,164
Status
Completed
Type
Research Grant
Start date
01/11/2000
End date
01/08/2004
Duration
45 months
Abstract
The study will focus on several important issues that remain to be resolved in relation to the binding of HMG1,2 to DNA and chromatin. The main emphasis will be on the distinguishing features of HMG1 and 2, viz. tandem HMG boxes and a long acidic tail. Particular aspects include: the nature of the cooperative binding of tandem HMG boxes to be the highest- affinity DNA substrate (minicircles); how tandem HMG boxes bind to linear DNA; how (whether) the acidic tail interacts with the rest of the protein (HMG boxes, linkers); and how the tandem HMG boxes and the acidic tail are involved in chromatic binding. We will also assess the importance of the two acetylatable lysine residues in the N-terminal strand of the A domain of the HMG1 for DNA binding.
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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