People

Dragony Fu

People

Contact Information

Dragony Fu
Assistant Professor
Office: Hutchison 333
Office Hours: By appointment
Phone: (585) 276-3346
Email: dragonyfu@rochester.edu
Lab Website
Research Interests: DNA repair mechanisms; Genotoxic stress response pathways; Programmed cell death  

Research Overview

  • Nucleic acid modification and repair
  • Cellular stress response pathways
  • Methyltransferases and dioxygenases

Our laboratory investigates the cellular roles of nucleic acid modification enzymes in biological processes ranging from neurodevelopment to the cellular stress response. In particular, we focus on discovering the targets and functions of two classes of enzymes: the SAM-dependent methyltransferases and the iron-dependent AlkB dioxygenases. To study the diverse processes modulated by these enzymes, we use an integrated biochemical, molecular and genetic approach in mammalian tissue culture systems as well as mouse knockout models. Through this approach, we have discovered novel targets and functions for enzymes involved in DNA repair, RNA modification and regulated cell death. The pathways and mechanisms identified through our studies provide critical insight into multiple aspects of human health and disease, including anti-cancer chemotherapy, degenerative disorders and aging.


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Selected Publications

  • Fu, D., Jordan, J. J. and Samson, L. D. (2013). "Human ALKBH7 is required for alkylation and oxidation-induced programmed necrosis." Genes & Development 27(10): 1089-1100.
  • Fu, D., Calvo, J. A. and Samson, L. D. (2012). "Balancing repair and tolerance of DNA damage caused by alkylating agents."Nature Reviews Cancer 12(2): 104-120.
  • Fu, D. and Samson, L. D. (2011). "Direct repair of 3,N(4)-ethenocytosine by the human ALKBH2 dioxygenase is blocked by the AAG/MPG glycosylase." DNA Repair.
  • Fu, D., Brophy, J. A., Chan, C. T., Atmore, K. A., Begley, U., Paules, R. S., Dedon, P. C., Begley, T. J. and Samson, L. D. (2010). "Human AlkB homolog ABH8 Is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival." Molecular and Cellular Biology 30(10): 2449-2459.
  • Errington, T. M., Fu, D., Wong, J. M. and Collins, K. (2008). "Disease-associated human telomerase RNA variants show loss of function for telomere synthesis without dominant-negative interference." Molecular and Cellular Biology 28(20): 6510-6520.
  • Fu, D. and Collins, K. (2007). "Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation." Molecular Cell 28(5): 773-785.
  • Fu, D. and Collins, K. (2006). "Human telomerase and Cajal body ribonucleoproteins share a unique specificity of Sm protein association." Genes & Development 20(5): 531-536.
  • Fu, D. and Collins, K. (2003). "Distinct biogenesis pathways for human telomerase RNA and H/ACA small nucleolar RNAs."Molecular Cell 11(5): 1361-1372.