People

Research Assistant Professor

My research has been focused on transcription mechanisms since my graduate studies and postdoc straining with Dr. Robert G. Roeder at Rockefeller University. In Dr. Chiang’s laboratory, I expanded the purification and reconstitution of the human general transcription machinery and general cofactors, first initiated in the Roeder Lab, with bacterially expressed recombinant human proteins (TFIIA, TFIIB, TBP, TFIIE, TFIIF, PC4) and with FLAG-tagged multiprotein complexes (TFIID, TFIIH, non-phosphorylated or hyper-phosphorylated RNA polymerase II, and different forms of Mediator complexes) purified from human HeLa cells expressing an epitope-tagged subunit of a multiprotein complex. The availability of this reconstituted transcription system with DNA or chromatin templates allows me to define the mechanisms of eukaryotic transcription regulated by different transcriptional regulators, e.g., p53, activator protein-1 (AP-1), and human papillomavirus (HPV)-encoded E2 proteins.  My recent establishment of in vitro modification assays with recombinant human enzymes for phosphorylation, acetylation, methylation, sumoylation, and ubiquitination studies expands a new line of research for defining the complexity of gene regulation involving chromatin and post-translational modification. I also conduct cell-based assays with both gain- and loss-of-function approaches to verify and discover new transcription mechanisms in living cells. Recently, I have employed genome-wide ChIP-seq/CUT&RUN and RNA-seq/PRO-seq approaches to define the functional roles of BRD4 protein isoforms and their transcriptional coregulators in different types of breast cancer cells and HPV-containing keratinocytes. I am also applying proteomics to identify protein-protein interactomes and drug targets.