Research overview
The attachment of the small protein, ubiquitin, to target proteins regulates a vast array of biological processes. We are interested in the role of ubiquitination in regulating transcription and the DNA damage response. We study the protein complexes that attach, recognize and remove ubiquitin modifications, as well as the way in which cross-talk between ubiquitination and other post-translational modifications regulates chromatin activity. We use x-ray crystallography, cryo-EM, enzymology, cell-based assays and a variety of biophysical tools to gain insights into the mechanisms underlying these essential cellular processes. Below is a summary of ongoing research projects:
The 1.9 MDa yeast SAGA complex has been a paradigm for understanding the connection between histone modifications and gene activation as well as the cross-talk between different types of modifications.
Monoubiquitination of histone H2B (H2B-Ub) plays a role in transcription, DNA replication and the DNA damage response. H2B-Ub is a rapidly turned over histone mark that is found in actively transcribed regions.
