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
Mais sinopses sobre JMJD6 é uma Dimetilase da Arginia da Histona