The JmjN and JmjC domains are two non-adjacent domains which have beenidentified in the jumonji family of transcription factors. Although it wasoriginally suggested that the JmjN and JmjC domains always co-occur and mightform a single functional unit within the folded protein, the JmjC domain waslatter found without the JmjN domain in organisms from bacteria to human[1, 2].

Proteins containing JmjC domain are predicted to be metalloenzymes that adopt the cupin fold and are candidates for enzymes that regulate chromatin remodelling [3]. The cupin fold is a flattened beta-barrel structure containing two sheets of five antiparallel beta strands that form the walls of a zinc-binding cleft. Based on the crystal structureof JmjC domain containing protein FIH and JHDM3A/JMJD2A, the JmjC domain forms an enzymatically active pocket that coordinates Fe(III) and alphaKG. Three amino-acid residues within the JmjC domain bind to the Fe(II) cofactor and twoadditional residues bind to alphaKG [3].

JmjC domains were identified in numerous eukaryotic proteins containing domains typical of transcription factors, such as PHD, C2H2, ARID/BRIGHT and zinc fingers [4, 4]. The JmjC has been shown to function in a histone demethylation mechanism that is conserved from yeast to human [5]. JmjC domain proteins may be protein hydroxylases that catalyse a novel histone modification [6]. The human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation [7].

1. Evidence of domain swapping within the jumonji family of transcription factors. Trends Biochem. Sci. 25, 274-6
2. JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta. Trends Biochem. Sci. 26, 7-9
3. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 7, 715-27
4. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. J. Biol. Chem. 278, 1802-6
5. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439, 811-6
6. Methylation: lost in hydroxylation? EMBO Rep. 6, 315-20
7. Expanding role of the jumonji C domain as an RNA hydroxylase. J. Biol. Chem. 285, 34503-7

The JmjN and JmjC domains are two non-adjacent domains which have beenidentified in the jumonji f
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