JMJD6 is a histone arginine demethylase

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

Research output: Contribution to journalArticle

423 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)444-447
Number of pages4
JournalScience
Volume318
Issue number5849
DOIs
StatePublished - Oct 19 2007

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    Chang, B., Chen, Y., Zhao, Y., & Bruick, R. K. (2007). JMJD6 is a histone arginine demethylase. Science, 318(5849), 444-447. https://doi.org/10.1126/science.1145801