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Science 8 October 2004:
Vol. 306. no. 5694, p. 193
DOI: 10.1126/science.306.5694.193n
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Enzymes that covalently modify histones generally come in pairs that have opposing effects on gene expression, such as acetylases and deacetylases or kinases and phosphatases. One notable exception are the enzymes that methylate histones on lysine or arginine residues. No enzymes had been identified that remove these potent and very stable epigenetic marks, until now. Wang et al. (p. 279, published online 2 September 2004) show that the enzyme peptidylarginine deiminase 4 (PAD4), which converts unmodified arginine residues to citulline in histones, can also convert methylated arginine residues in histones to citrulline, thereby removing the methyl mark ("demethylimination"). PAD4 can modulate the expression of genes known to be regulated by arginine histone methylases, which suggests that at least one of the elusive histone demethylases may have been identified.




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Science. ISSN 0036-8075 (print), 1095-9203 (online)