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Methylation: lost in hydroxylation?
Author(s) -
Trewick Sarah C.,
McLaughlin Paul J.,
Allshire Robin C.
Publication year - 2005
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400379
Subject(s) - demethylase , histone methylation , histone methyltransferase , histone , chromatin , histone code , histone h3 , histone h2a , biochemistry , biology , methylation , protein methylation , histone h1 , chemistry , microbiology and biotechnology , dna methylation , methyltransferase , nucleosome , gene , gene expression
Methylation of histone tails is a key determinant in forming active and silent states of chromatin. Histone methylation was regarded as irreversible until the recent identification of a lysine‐specific histone demethylase (LSD1), which acts specifically on mono‐ and dimethylated histone H3 lysine 4. Here, we propose that the fission yeast protein Epe1 is a putative histone demethylase that could act by oxidative demethylation. Epe1 modulates the stability of silent chromatin and contains a JmjC domain. The Epe1 protein can be modelled onto the structure of the 2‐oxoglutarate‐Fe(II)‐dependent dioxygenase, factor inhibiting hypoxia inducible factor (FIH), which is a protein hydroxylase that also contains a JmjC domain. Thus, Epe1 and certain other chromatin‐associated JmjC‐domain proteins may be protein hydroxylases that catalyse a novel histone modification. Another intriguing possibility is that, by hydroxylating the methyl groups, Epe1 and certain other JmjC‐domain proteins may be able to demethylate mono‐, di‐ or trimethylated histones.