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Efforts to Elucidate the Molecular Basis of the Interaction between LSD1 and CoREST: The Expression and Purification of CoREST
- Abstract:
Modulating the activity of proteins that interact with modification of histone tails is a viable approach to control pathological problems. CoREST, a co-repressor protein, stimulates the histone demethylation activity of LSD1 (Lysine-Specific Demethylase 1), one of the transcriptional repressor complexes that is involved in cancer progression. An understanding of the binding of CoREST to LSD1 can be crucial in the development of inhibition of this complex. Inhibition of this complex may result in the downregulation of histone demethylation via the sequestering of LSD1. Prior to the characterization of the binding, both CoREST and the functional region of CoREST (Δ286-CoREST) have been expressed and purified. The solubility of these proteins has been enhanced by growing cells at low temperature with an enriched medium, which shows promise for future studies by reducing the formation of insoluble aggregates. The analysis of binding between LSD1 and Δ286-CoREST, the mutation of key residues of Δ286-CoREST that contribute to the complex formation, and the examination of the role of Δ286-CoREST on LSD1 activity in vivo will allow us to develop strategies to inhibit LSD1 activity.
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