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Ray Trievel

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Primary Appointment: Biological Chemistry Dept
Other PIBS Depts.: Biophysics
PubMed Name: Trievel RC
Department Website

  Protein covalent modifications play a pivotal role in orchestrating a myriad of cellular functions. Our laboratory is interested in understanding the mechanisms by which protein modifications within the nucleus impact transcription and other genomic processes. Histones are the major scaffolding proteins that organize genomic DNA into a nucleoprotein complex termed chromatin and are subject to an array of modifications that includes acetylation, methylation, phosphorylation, sumoylation, and ubiquitination. Transcription factors and protein subunits comprising the basal transcription machinery undergo analogous modifications that control their functions. These modifications act either individually or combinatorially to regulate transcription, DNA repair, replication, recombination, and other genomic processes and are believed to represent a heritable epigenetic code that governs cell identity and fate. Aberrant modification patterns have been linked to cancer and other diseases, underscoring the fundamental importance of these pathways in governing faithful gene expression.

Our primary research goals are to elucidate the molecular mechanisms of enzymes that catalyze chromatin modifications and the specificities of effector proteins that recognize these modifications to transduce the information encoded by these marks. In addition, we are developing biochemical assays and other reagents to facilitate high throughput screening of small molecule inhibitors against chromatin modifying enzymes. Together, these efforts will yield new insights into the biological mechanisms underlying chromatin modifications and will furnish a framework for developing novel therapeutics designed to treat cancer and other modification-linked diseases.