The Chatterjee lab develops new chemical tools to investigate the mechanistic roles of protein post-translational modifications in human gene regulation. The chemical modifications we study vary in complexity from the methylation and acetylation of lysine side-chains to their conjugation with small proteins, such as ubiquitin and the small ubiquitin-like modifier protein (SUMO).1 By employing a powerful combination of synthetic protein chemistry and molecular biology, called semisynthesis, we have produced uniformly and site-specifically ubiquitylated and sumoylated human histones and transcription factors in quantities that are inaccessible from cells.2,3 Biophysical and biochemical studies with these proteins have revealed the direct effects of sumoylation on chromatin structure and function, and identified new biochemical crosstalk between histone sumoylation and methylation.4 The semisynthetic methodologies and insights gained from mechanistic studies with modified histones will be presented and discussed in the context of RNA polymerase II-mediated gene transcription.
Speaker: Champak Chatterjee, Univ. of Washington
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