A Neutron Scattering Solution Study of Chromatin Regulatory Proteins in the Human Malaria Parasite
This proposal concerns the malaria parasite Plasmodium falciparum, investigating a key biomolecular interaction that is believed to be central to the way the parasite evades the human immune system. To do this, it expresses many virulence genes in a highly controlled manner. Our work focuses on protein-protein and protein-DNA interactions that regulate the expression of these genes. The P. falciparum virulence genes are controlled epigenetically, by histone marks that activate or silence their expression. A key player in this is the 'sirtuin' histone deacetylase enzyme, PfSir2a. The enzyme is unlikely to bind DNA directly, but was recently shown to interact with a small DNA-binding protein called PfAlba3. We will use SANS methods, together with selective deuteration, to determine the solution structures of the sirtuin-alba complex. The work will improve our understanding of the basic biology of the human malaria parasite and the impact of this biology on virulence.
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JORDAN Ashley; Juliette M. Devos; FORSYTH Victor Trevor; HAERTLEIN Michael; MARTEL Anne; MERRICK Catherine; MITCHELL Edward and PORCAR Lionel. (2014). A Neutron Scattering Solution Study of Chromatin Regulatory Proteins in the Human Malaria Parasite. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-827
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