Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 12 October 2004
Vol. 2004, Issue 254, p. tw368
[DOI: 10.1126/stke.2542004tw368]

EDITORS' CHOICE

GENE METHYLATION Removing Epigenetic Marks

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. Notable exceptions 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. show that the enzyme peptidylarginine deiminase 4 (PAD4), which converts unmodified arginine residues to citrulline 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.

Y. Wang, J. Wysocka, J. Sayegh, Y.-H. Lee, J. R. Perlin, L. Leonelli, L. S. Sonbuchner, C. H. McDonald, R. G. Cook, Y. Dou, R. G. Roeder, S. Clarke, M. R. Stallcup, C. D. Allis, S. A. Coonrod, Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 306, 279-283 (2004). [Abstract] [Full Text]

Citation: Removing Epigenetic Marks. Sci. STKE 2004, tw368 (2004).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882