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Sean Taverna

410-502-0790 (p)
Sean Taverna

Pharmacology and Molecular Sciences IBBS Epigenetics Center Histone and chromatin modifications, epigenetics and gene function, identification of histone binding modules, and small RNA directed gene silencing


Assistant Professor

Research Summary

Eukaryotic cells package their genomes in the form of chromatin, which is comprised of histone proteins and DNA. Modification of chromatin by chemical marks such as methylation and acetylation affects how cellular machineries interpret the genome. The Taverna laboratory studies how histone marks contribute to an “epigenetic/histone code” that may dictate chromatin-templated functions like transcriptional activation and gene silencing, as well as how these On/Off states are inherited/ propagated. For example, transcription-modulating protein complexes with PHD finger motifs (methyl lysine “readers”) or Bromodomains (acetyl lysine “readers”) often have enzymatic activities that “write” these same histone marks. To explore these connections we use biochemistry and cell biology in a variety of model organisms ranging from mammals to yeast and ciliates. The lab also investigates links between small RNAs and histone marks involved in gene silencing. Importantly, many histone binding proteins have clear links to human disease, notably leukemia and other cancers.


Journal Citations

Gradolatto, A.; Smart, S.K.; Byrum, S.; Blair, L.P.; Rogers, R.S.; Kolar, E.A.; Lavender, H.; Larson, S.K.; Aitchison, J.D.; Taverna, S.D.; Tackett, A.J. A noncanonical bromodomain in the AAA ATPase protein Yta7 directs chromosomal positioning and barrier chromatin activity. Mol Cell Biol. 2009 Sep;29(17):4604-4611.
Smart, S.K.; Mackintosh, S.G.; Edmondson, R.D.; Taverna, S.D.; Tackett, A.J. Mapping the local protein interactome of the NuA3 histone acetyltransferase. Protein Sci. 2009 Sep;18(9):1987-1997.


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