Benny Howard
Structural and functional studies on the G3842S mutation in the Mixed Lineage Leukemia protein (MLL)
The Mixed Lineage Leukemia (MLL) protein is a histone H3 methyltransferase that methylates lysine 4 on histone H3, which an epigenetic signal for transcriptional activation (Strahl et al. 2000). The genes MLL positively regulates are Hox genes, which are homeotic regulators of development (Wiederschain et al. 2003). The Mixed Lineage Leukemia (MLL) protein is mutated in 5 to 10% of children and adults that have acute lymphoblastic leukemia (Canaani et al., 2004). The prognosis of those cancer patients is poor (Pui et al., 2002). The purpose of this study is to provide an understanding of how MLL functions in order to help facilitate the development of new cancer treatments, which could improve the prognosis of individuals with MLL related leukemia. This will be done by studying the Trithorax Z11 (TRX Z11) mutation in MLL. Doing this will show how a critical amino acid affects the function and structure of MLL.
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