Dr. Taverna and the Taverna Laboratory study 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 they 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.
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Blair LP, Avaritt NL, Huang R, Cole PA, Taverna, SD, Tackett AJ. “MassSQUIRM: An assay for quantitative measurement of lysine demethylase activity.” Epigenetics. 6(4), 490-499, 2011.
Taverna SD, Cole PA. “Drug discovery: Reader's block.” Nature. 468, 1050-1051, 2010.
Gradolatto A, Smart SK, Byrum S, Rogers RS, Lavender H, Kolar E, Aitchison JD, Taverna SD, and Tackett AJ. “A noncanonical bromodomain in the AAA ATPase protein Yta7 directs chromosomal positioning and barrier chromatin activity.” Mol Cell Bio, 2009.
Smart SK, Mackintosh SG, Edmondson RD, Taverna SD, Tackett AJ. “Mapping the local protein interactome of the NuA3 histone acetyltransferase.” Protein Sci. 18, 1987-1997, 2009.
Taverna, S.D., Li, H., Ruthenburg, A.J., Allis, C.D. and Patel, D.J. “How chromatin binding modules interpret histone modifications.” Nat. Struct. Mol. Bio. 14:1025-1040, 2007.