Contact InformationOffice: WEL: 4.260B
LabOffice: WEL 4.258
Yan Jessie Zhangjzhang@cm.utexas.edu
PhD, The Scripps Research Institute, 2004
BS, Tsinghuan University, China, 1997
MS, University of Oregon, 2000
The Salk Institute for Biological Research
Structural and biophysical studies of enzymes in oncology pathways, structure-based drug design.
A major focus of Zhang's research is the elucidation of the fundamental principles of transcriptional regulation and their impact on tumor and stem cell differentiation. The primary experimental approaches used in the laboratory are macromolecular structure determination and allied biophysical techniques. The transcription of DNA information into mature RNA messages requires a temporally changing transcription apparatus, which is assembled from RNA polymerase II and various processing factors. The appropriate assembly of the transcription apparatus is governed by information programmed in the C-terminal domain (CTD) of RNA polymerase II. This so-called 'CTD code' operates through changes in the conformation of CTD, which are effected largely through alteration of the phosphorylation state of this domain. Zhang’s main research interests focus on how phosphorylation of CTD is regulated and how this phosphorylation affects the outcome of transcription, and in turn, how these processes are involved in important biological phenomena such as cancer and neurogenesis. Ultimately, Zhang aims to exploit the results from this research in the design of small molecule effectors that can intervene in the CTD processes and thereby function as regulators of gene expression.
Burks E.A., Yan W., Johnson Jr.,W H., Li W., Schroeder G.K., Min C., Gerratana B., Zhang Y., and Whitman C.P.
Kinetic, Crystallographic, and Mechanistic Characterization of TomN: Elucidation of a Function for a 4-Oxalocrotonate Tautomerase Homologuein the Tomaymycin Biosynthetic Pathway. Biochemistry. In press.
Lee TH, Chen CH, Suizu F, HuangP, Schiene-Fischer C, Daum S, Zhang Y, Goate A, Chen RH, Zhou XZ, Lu KP
Death-associated protein kinase1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellularfunction. Mol Cell. 2011 Apr22;42(2):147-59. Epub 2011 Apr 14
Zhang M, Cho EJ, Burstein G,Siegel D, Zhang Y
Selective inactivation of a human neuronal silencing phosphatase by a smallmolecule inhibitor. ACS Chemical Biol. 2011 May 20;6(5):511-9. Epub 2011 Feb 24. (Featured Cover May 2011, Featured story in Podcast May 2011)
Zhang Y, Zhang M, Zhang Y
Crystal Structure of Ssu72, an essential eukaryotic phosphatase specific forthe C-terminal domain of RNA polymerase II. Biochemical Journal. 2011, 2011 Feb 24;434(3):435-44.
Zhang M, Gill GN, Zhang Y
Biomolecular architects: A scaffold provided by the C-terminal domain ofeukaryotic RNA polymerase II. Nano Review 2010, 1: 5502. (Invited review)