Jumonji domain-containing protein

Function

Jumonji domain-containing protein 2A (Jmjd2a) catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36 producing the demethylated form. Jmjd2a domains contain: N-terminal, catalytic core (residues 1-350), 2 TUDOR domains which recognize dimethylated Arg (residues 895-1011) , 2 PHD-type zinc fingers and C-terminal domain. Jmjd2a is Fe+2 and α-ketoglutarate dependent. Methylation of histones in the chromatin is involved in regulation of gene activity, chromatin structure and epigenetic memory^[1].

Disease

Relevance

Structural highlights

Jmjd2a uses 9 residues for interaction with the methylated peptide and 4 residues are involved with binding to the peptide's trimethyllysine moiety. An O2 molecule is recruited into the catalytic center^[2].