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The high mobility group protein hmg-d - study of its interaction with dna and its biological function


Research objectives and content
HMG-D is one the Drosophila counterparts of the mammalian HMG- 1 and 2 proteins. These proteins are abundant and their function is not clearly determined. HMG-D comprises a single HMG domain, which is a DNA binding motif, followed by a basic region and a c-terminal acidic tail. The acidic tail of HMG-D confers the selectivity for deformed DNA structures and therefore modulates the binding of HMG-D to DNA. By NMR spectroscopy studies we will determine how the acidic tail works. We expect that the acidic tail modulates the structure of HMG-D by interacting with the HMG domain and therefore modulates its DNA binding. We suggest that the modification by phosphorylation of the acidic tail could provide a way for changing DNA binding affinity in vivo. The modifications of HMG-D and the DNA binding properties of the modified protein will be investigated. Finally we propose to test whether HMG-D acts as a DNA chaperone in the assembly of nucleosomes and higher DNA structures.
Training content (objective, benefit and expected impact)
This project will give me some training in: - NMR spectroscopy, protein structure. - biochemistry of proteins, purification of proteins from Drosophila embryos, in investigating the modification of proteins. - chromatin structure I will acquire some more experience in DNA-protein interaction and in molecular biology.
Links with industry / industrial relevance (22)

Funding Scheme

RGI - Research grants (individual fellowships)


MRC Laboratory of Molecular Biology
Hills Road
CB2 2QH Cambridge
United Kingdom

Participants (1)

Not available