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.
Science 19 October 2007:
Vol. 318. no. 5849, pp. 444 - 447