Cheng Laboratory

Xiaodong Cheng, Ph. D.

Professor

Eminent Scholar in X-Ray Crystallography


Xiaodong ChengMy research interests are mainly focused on epigenetic modifications of DNA methylation and histone modifications. Please see publications below:

Chang Y, Sun L, Kokura K, Horton JR, Fukuda M, Espejo A, Izumi V, Koomen JM, Bedford MT, Zhang X, Shinkai Y, Fang J, Cheng X. (2011) MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9. Nat Commun. 2: 533.

Estève PO, Chang Y, Samaranayake M, Upadhyay AK, Horton JR, Feehery GR, Cheng X, Pradhan S (2011) A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability. Nat Struct Mol Biol. 18, 42-48.

Levy D, Kuo, AJ, Chang Y, Schaefer U, Kitson C, Cheung P, Espejo A, Zee BM, Liu CL, Tangsombatvisit S, Tennen RI, Kuo AY, Tanjing S, Cheung R, Chua KF, Utz PJ, Shi X, Prinjha RK, Lee K, Garcia BA, Bedford MT, Tarakhovsky A, Cheng X, Gozani O (2011) Lysine methylation of the NF-kB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kB signaling . Nat Immunol. 12, 29-36.

Horton JR, Upadhyay AK, Qi HH, Zhang X, Shi Y, Cheng X. (2010) Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat Struct Mol Biol. 17, 38-43.

Chang Y, Zhang X, Horton JR, Upadhyay AK, Spannhoff A, Liu J, Snyder JP, Bedford MT, Cheng X (2009) Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294. Nat Struct Mol Biol. 16, 312-7.

Hashimoto H, Horton JR, Zhang X, Bostick M, Jacobsen SE, Cheng X (2008) The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix. Nature, 455, 826-829.

Subramanian K, Jia D, Kapoor-Vazirani P, Powell DR, Collins RE, Sharma D, Peng J, Cheng X, Vertino PM (2008) Regulation of estrogen receptor á by the SET7 lysine methyltransferase. Mol Cell 30, 336-347.

Rathert P, Dhayalan A, Murakami M, Zhang X, Tamas R, Jurkowska R, Komatsu Y, Shinkai Y, Cheng X, Jeltsch A (2008) Protein lysine methyltransferase G9a acts on non-histone targets. Nat Chem Biol. 4, 344-6.

Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X (2008) The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules. Nat Struct Mol Biol. 15, 245-50.

Jia D, Jurkowska RZ, Zhang X, Jeltsch A, Cheng X (2007) Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation. Nature, 449, 248-251.

Ooi SK, Qiu C, Bernstein E, Li K, Jia D, Yang Z, Erdjument-Bromage H, Tempst P, Lin SP, Allis CD, Cheng X, Bestor TH (2007) DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA. Nature, 448, 714-717.

Lan F, Collins RE, De Cegli R, Alpatov R, Horton JR, Shi X, Gozani O, Cheng X, Shi Y (2007) Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression. Nature, 448, 718-722.

J.R. Horton, K. Liebert, S. Hattman, A. Jeltsch, X. Cheng (2005) Transition from nonspecific to specific DNA interaction along the substrate recognition pathway of Dam methyltransferase. Cell, 121, 349-361.

X. Zhang, Z Yang, S.I. Khan, J.R. Horton, H. Tamaru, E.U. Selker, X. Cheng (2003) Structural Basis for the Product Specificity of Histone Lysine Methyltransferases. Molecular Cell 12, 177-185.

Yang Z, Horton JR, Zhou L, Zhang XJ, Dong A, Zhang X, Schlagman SL, Kossykh V, Hattman S, Cheng X (2003) Structure of the bacteriophage T4 DNA adenine methyltransferase. Nature Struct. Biol. 10, 849-855.

Tamaru H, Zhang X, McMillen D, Singh P, Nakayama J, Grewal S, Allis D, Cheng X, Selker EU (2003) Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in Neurospora crassa. Nature Genetics 34, 75-79.

X. Zhang, H. Tamaru, S. I. Khan, J. R. Horton, L. J. Keefe, E. U. Selker, X. Cheng (2002) Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell 111, 117-127.
C. Qiu, K. Sawada, X. Zhang, X. Cheng (2002) The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds. Nature Struct. Biol. 9, 217-224.

Current Members of the Cheng Lab:

Hideharu Hashimoto
Research Associate
 
Sam Hong
Grad Student
shong27@emory.edu
 
John R. Horton
Assistant Professor
 
Justin Jones
Postdoctoral Fellow
 
Satish Kallappagoudar
Postdoctoral Fellow
 
Yusuf Olanrewaju
Research Specialist
 
Anamika Patel
Assistant Professor
 
Xing Zhang
Assistant Professor
 

Contact Information

Department of Biochemistry
1510 Clifton Rd. NE
Atlanta, GA 30322

O. Wayne Rollins Center
G254 Office
G239 Lab
404.727.8491 (Office tel.)
404.727.8492 (Lab tel.)
404.727.3746 (Fax)
xcheng@emory.edu