Research in my group focuses on the molecular mechanisms of epigenetic regulation and phosphoinositide signaling. We apply high field NMR spectroscopy, X-ray crystallography and a wide array of biochemical and molecular biology approaches to characterize the atomic-resolution structures and functions of chromatin- and lipid-binding proteins implicated in cancer and other human diseases.

The study of epigenetics and deciphering the ‘epigenetic code/language’ is the major direction in the lab. The genetic material of eukaryotic cells is packaged into the nucleus in the form of chromatin. Chromatin is made up of building blocks called nucleosomes. Each nucleosomal particle contains an octamer of four histone proteins, H2A, H2B, H3 and H4, around which genomic DNA is wound almost twice. The nucleosomes undergo recurrent structural rearrangements and are subject to posttranslational modifications (PTMs). A particularly large number of PTMs, or epigenetic marks, have been identified on the histone tails that protrude from the nucleosomal core and are freely accessible to histone acetyltransferases (HATs), histone deacetylases (HDACs), histone lysine methyltransferases (HKMTs), kinases, phosphatases and other enzymes capable of depositing or removing PTMs. The list of PTMs is expanding rapidly and includes, among others, acetylation and methylation of lysine residues, methylation of arginine residues, and phosphorylation of serine and threonine residues.