Journal
SCIENCE
Volume 318, Issue 5849, Pages 444-447Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1145801
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Funding
- NCI NIH HHS [CA107943, CA115962] Funding Source: Medline
- NCRR NIH HHS [C06-RR15437-01] Funding Source: Medline
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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.
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