Xiaodong Cheng Ph.D.

Georgia Research Alliance Eminent Scholar
Professor of Biochemistry at Emory University School of Medicine, Atlanta, Georgia

Dr. Xiaodong Cheng is a Georgia Research Alliance Eminent Scholar and Professor of Biochemistry at Emory University School of Medicine, Atlanta, Georgia. He was educated in China (B.Sc., Fudan University, 1982) and moved to the USA, where he received a Ph.D. in Protein Crystallography in 1989. He subsequently moved to Cold Spring Harbor Laboratory in 1990, reaching the position of Senior Staff Investigator. It was in Cold Spring Harbor where he began a fruitful research collaboration with Dr. Richard J. Roberts (a Nobel Prize winner in 1993) that led to the discovery of DNA base flipping. In 1997, he moved to Emory and his current work focuses on epigenetic methylation.
Dr. Cheng’s group determined the first structure of a protein arginine methyltransferase (2000 EMBO J), the first structure of a histone lysine methyltransferase (2002 Cell), established a switch mechanism of Phe/Tyr (phenylalanine/tyrosine) in controlling the degree of lysine methylation by one, two or three methyl groups (2003 Mol. Cell), and illustrated the transition from nonspecific to specific DNA interaction along the substrate recognition pathway by a DNA methyltransferase (2005 Cell). In collaboration with a group of scientists, Dr. Cheng’s group used elegant structural and biochemical analyses that provide insights into the long-standing question of how imprinted genes are targeted for DNA methylation (2007 three Nature papers). They revealed a novel mechanism of converting patterns of histone methylation into patterns of DNA methylation that mediate the heritable silencing, and the underlying DNA sequences of imprinted genes also contribute to the establishment of heritable methylation patterns. More recently, his group demonstrated that an ankyrin repeat domain bind selectively to mono- and dimethylated lysine 9 of histone H3 (2008 Nature Structural & Molecular Biology), a recognition of hemi-methylated CpG by SRA domain using a base-flipping mechanism (2009 Nature), and a structural basis for inhibition of G9a protein lysine methyltransferase by BIX-01294 (2009 Nature Structural & Molecular Biology).

Talk Title: “Epigenetic link between DNA methylation and histone modifications”