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PMID:17947579
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| Citation |
Chang, B, Chen, Y, Zhao, Y and Bruick, RK (2007) JMJD6 is a histone arginine demethylase. Science 318:444-7 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1126/science.1145801 |
| Keywords |
Amino Acid Sequence; Arginine/metabolism; HeLa Cells; Histones/metabolism; Humans; Jumonji Domain-Containing Histone Demethylases; Methylation; Molecular Sequence Data; Oxidation-Reduction; Protein Processing, Post-Translational; Receptors, Cell Surface/chemistry; Receptors, Cell Surface/genetics; Receptors, Cell Surface/metabolism; Recombinant Proteins/metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
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