Department Affiliation: Primary: Pharmacology and Molecular Sciences; IBBS Epigenetics Center
Degree: Ph.D., University of Virginia
Rank: Assistant Professor
Telephone Number: 410-502-0790
Lab Number: 410-955-1119
Fax Number: 410-955-3023
E-mail address: staverna@jhmi.edu
School of Medicine Address: Room 575, John G. Rangos, Sr., Building, 855 N. Wolfe Street, Baltimore, MD 21205
Histone and chromatin modifications, epigenetics and gene function, identification of histone binding modules, and small RNA directed gene silencing
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.
Representative Publications:
Jacobs S.A., Taverna. S.D., Zhang, Y., Briggs, S.D., Li, J., Eissenberg, J.C., Allis, C.D., and Khorasanizadeh, S. (2001) Specificity of the HP1 chromodomain for the methylated N-terminus of histone H3. EMBO J. 20:5232-5241, 2001. Pub Med Reference
- Taverna S.D., Coyne, R.S., and Allis, C.D. Methylation of histone H3 at lysine 9 targets programmed DNA elimination in Tetrahymena. Cell 110:701-711, 2002. Pub Med Reference
- Taverna, S.D., Ilin, S., Rogers, R.S., Tanny, J.C., Lavender, H., Li, H., Baker, L., Boyle, J., Blair, L.P., Chait, B.T., Patel, D.J., Aitchison, J.D., Tackett, A.J., and Allis, C.D. Yng1 PHD finger binding to histone H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Molecular Cell. 24:785-796, 2006. Pub Med Reference
- Taverna, S.D., Ueberheide, B.M., Liu, Y., Tackett, A.J., Diaz, R., Shabanowitz, J., Chait, B.T., Hunt, D.F. and Allis, C.D. Long-distance combinatorial linkage between methylation and acetylation on H3 N-termini. Proc. Natl. Acad. Sci. USA. 104:2086-2091, 2007. Pub Med Reference
- 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. Pub Med Reference
- 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); 29(17):4604-11. PMC2725702 Pub Med Reference
- Smart SK, Mackintosh SG, Edmondson RD, Taverna SD†, and Tackett AJ†. Mapping the local protein interactome of the NuA3 histone acetyltransferase. Protein Science (2009); 18(9):1987- 1997. Pub Med Reference
Other graduate programs in which Dr. Taverna participates:
