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Investigating Roles of Reader Domains in Regulating Activity of Jumonji Histone Demethylases
Author(s) -
Fujimori Danica Galonic
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.337.2
Subject(s) - histone methyltransferase , chromatin , histone , nucleosome , biochemistry , histone methylation , biology , methyltransferase , methylation , chemistry , microbiology and biotechnology , dna methylation , dna , gene expression , gene
Methylation of histones, protein subunits of nucleosome particles within chromatin, has a profound impact on regulation of transcription. This post‐translational modification is controlled by opposing action of histone methyltransferases and histone demethylases, enzymes that install and remove histone methyl marks, respectively. Jumonji histone demethylases are Fe(II)‐ and alpha‐ketoglutarate‐ dependent oxygenases that remove methyl marks from side chain amino groups of lysines. It is postulated that, in analogy to other members of the superfamily, demethylation proceeds by a radical mechanism where hydrogen atom abstraction from the methyl group, followed by oxygen rebound, results in the formation of a hemiaminal intermediate which fragments to release formaldehyde and demethylated product. The precise control of the activity of demethylases is crucial, and misregulation of demethylation is associated with various human diseases. In addition to a catalytic domain that harbors the iron binding site, several families of demethylases also contain reader domains which recognize chromatin modifications. In this talk, our finding on regulation of the catalytic activity of jumonji histone demethylases by their reader domains will be presented.