Faculty Profile
 
  ZANG Jianye
     
Department: School of Life Science
Mailing Address:
School of life science, University of Science and Technology of China,96 Jinzhai Road, Hefei, Anhui, 230027, China
Postal Code:
230027
Phone:
+86-551-63603433
Fax:
86-551-63603433
Homepage:
http://biox.ustc.edu.cn/szdw/szkxybrjh/201006/t20100626_22931.html
 
       

Research Profile

Jianye Zang, Ph. D.
Professor, Selected into CAS “Hundred Talents Program”,
School of life science,
University of Science and Technology of China,
96 Jinzhai Road, Hefei, Anhui, 230027, China
Email: zangjy@ustc.edu.cn

Education:

B.S., Chemistry, Department of Material Science and Engineering  University of Science and Technology of China, 1998
Ph.D., Structural Biology, Department of Molecular and Cell Biology, University of Science and Technology of China, 2003

Research Interest:

Covalent modifications of histone, including methylation, acetylation, phosphorylation, ubiquitination, and so on, are crucial for various biological processes. The same modification read by different “readers” will produce different biological outcomes. Each modification is dynamically controlled by the interplay of "writers" with "erasers", which may be established when special signal presents. After establishment, some of these modifications are able to be maintained at specific site and are inheritable, even if the triggering signals disappeared. In addition, enzymatic activities of the enzymes participating in modification of histones are tightly regulated. We are interested in the mechanisms of recruitment of these enzymes to target genes. The mechanisms of enzymatic activity regulation are also interesting question to us. We will use X-ray crystallographic, biochemical,molecular biology and other biophysical techniques to explore these fascinating questions. 

 
     
Selected Publications
1) Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. , EMBO J. , 2011 , 30, 2829-42.
2)  Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus , J Struct Biol. , 2011 , 174(2): 413-9.
3) Interaction of JMJD6 with single-stranded RNA , Proc. Natl. Acad. Sci. USA , 2010 , 107, 14568-72.
4) Solution NMR characterization of Sgf73(1-104) indicates that Zn ion is required to stabilize zinc finger motif. , Biochem. Biophys. Res. Commun. , 2010 , 397, 436-40.
5) A biosynthetic route to photoclick chemistry on proteins. , J. Am. Chem. Soc. , 2010 , 132, 14812-8.
6) Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing , J. Biol. Chem. , 2010 , 285, 4251-62.
7) Structural basis of the recognition of a methylated histone tail by JMJD2A , Proc. Natl. Acad. Sci. USA. , 2007 , 104, 10818-23
8) Structural insights into histone demethylation by JMJD2 family members , cell , 2006 , 125, 691-702
 
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