Yan Jessie Zhang

Zhang, Yan Jessie
Assistant Professor in Chemistry & Biochemistry

E-mail: jeszhang@mail.utexas.edu

Website: http://zhang.cm.utexas.edu/

Main Office: WEL 4.260B
Phone: 471-8645

Alternate Office: WEL 4.258
Phone: 471-1027

Mailing Address:
1 University Station A5300
Austin, TX 78712
Research Summary:
   A major focus of Zhang's research is the elucidation of the fundamental principles of transcriptional regulation. 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. My 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, 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.
 
Research Images:

- Small carboxyl-terminal domain phosphatases (Scp1-3) have been recently identified and shown to specifically dephosphorylate the phosphorylated Ser5 position of the tandem repeats of CTD. More importantly, Scp phosphatases are recruited by the repressor element 1 (RE-1)-silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) complex to non-neuronal cells to mediate neuronal gene silencing. Shown is the CTD peptide of RNA polymerase II bound to the Scp1 active site. Residues identical between Scp1 and its homologue Fcp1 are colored orange; chemically similar residues are colored pink. Phe106, a key specificity determinant of Scp1 dephosphorylation of P.Ser5, is highlighted in yellow.

 
Publications:
Crystal Structure of Ssu72, an essential eukaryotic phosphatase specific for the C-terminal domain of RNA polymerase II (2011) Biochemical Journal., In press.
Biomolecular architects: A scaffold provided by the C-terminal domain of eukaryotic RNA polymerase II. (2010) Nano Review 1, 5502 .
Structural and Functional Analysis of the Phosphoryl Transfer Reaction Mediated by the Human Small C-terminal Domain Phosphatase, Scp1. (2010) Protein Sci. 19(5), 974-86.
Structural basis for high affinity peptide based inhibition of human Pin1 (2007) ACS Chem. Biol 2(5), 320-328.
Preferential dephosphorylation of CTD by Scp1: complex structure of phosphatase Scp1 with CTD of RNA Polymerase II (2006) Mol Cell 24, 759-770.
Structure-function-folding relationship in a WW domain (2006) Proc Natl Acad Sci U S A. 103(28), 10648-10653..

 
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