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Science 19 October 2007:
Vol. 318. no. 5849, pp. 444 - 447
DOI: 10.1126/science.1145801
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Reports

JMJD6 Is a Histone Arginine Demethylase

Bingsheng Chang, Yue Chen, Yingming Zhao, Richard K. Bruick*

Arginine methylation occurs on a number of proteins involved in a variety of cellular functions. Histone tails are known to be mono- and dimethylated on multiple arginine residues where they influence chromatin remodeling and gene expression. To date, no enzyme has been shown to reverse these regulatory modifications. We demonstrate that the Jumonji domain–containing 6 protein (JMJD6) is a JmjC-containing iron- and 2-oxoglutarate–dependent dioxygenase that demethylates histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) in both biochemical and cell-based assays. These findings may help explain the many developmental defects observed in the JMJD6–/– knockout mice.

Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390–9038, USA.

* To whom correspondence should be addressed. E-mail: richard.bruick{at}utsouthwestern.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)