Jessie Zhang

Email: jeszhang@mail.utexas.edu

A major focus of our 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. Our 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.

The primary experimental approaches used in the laboratory are macromolecular structure determination and allied biophysical techniques. Ultimately, we aim 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.

References:

Zhang Y, Daum S, Wilderman D, Zhou XZ, Verdecia MA, Bowman ME, Hunter T, Lu KP, Fischer G, Noel JP. Structural basis for high affinity peptide based inhibition of human Pin1 ACS Chem. Biol. 2007 May 18, 2 (5), 320â“328 (Featured by ACS as Most Cited 2007).

Zhang Y, Kim Y, Genoud N, Gao J, Kelly JW, Pfaff SL, Gill GN, Dixon JE and Noel JP Preferential dephosphorylation of CTD by Scp1: complex structure of phosphatase Scp1 with CTD of RNA Polymerase II Mol Cell, 2006 Dec 8; 24: 759-70.

Jager M*, Zhang Y*, Nguyen H, Dendle G, Bowman ME, Gruebele M, Kelly JW. Structure-function-folding relationship in a WW domain. Proc Natl Acad Sci U S A. 2006 Jul 11;103 (28):10648-53.

 

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