2018年3月30日 · Using the powerful bimolecular fluorescence complementation technique, we herein show the in situ formation of human KDM4A and KDM4C homodimers and heterodimers in nuclei of live transfectant cells and evaluate their H3K9me3 demethylation activity.

Here, we reveal that the JmjN and JmjC domains interact with each other through two β-sheets, one in each domain. Removal of either or both β-strands or the entire JmjN domain leads to complete degradation of Gis1, mediated partially by the proteasome.

Recent studies have identified Jhd2, a JmjC domain-containing protein, as an H3K4-specific demethylase in budding yeast. However, important questions regarding the regulation and functions of Jhd2 remain unanswered.

2018年3月30日 · The JmjN domain was found as both essential and sufficient for dimerization, since its deletion in KDM4C abolished the enzyme’s dimerization capacity, while the individual JmjN peptide formed homodimers.

2020年10月2日 · To date, this domain always co-occurs with the JmjC domain (although the reverse is not true). smart00545 is a member of the superfamily cl15840. Jiyao W et al. (2023). "The conserved domain database in 2023.", Nucleic Acids Res. 51 (D1):D384-D388.

2015年6月1日 · The JmjN domain is shown to be an integral core of all KDM catalytic domains. The Jumonji (Jmj) family of demethylases has a crucial role in regulating epigenetic processes through the removal of methyl groups from histone tails.

2007年3月7日 · JmjC-domain-containing proteins encode a family of histone lysine demethylases that can remove all three methylation states. Members of this family have been shown to catalyse the removal...

2010年8月6日 · Recent studies have identified Jhd2, a JmjC domain-containing protein, as an H3K4-specific demethylase in budding yeast. However, important questions regarding the regulation and functions of Jhd2 remain unanswered.

JmJC domains are predicted to be metalloenzymes that adopt the cupin fold, and are candidates for enzymes that regulate chromatin remodelling. The cupin fold is a flattened beta-barrel structure containing two sheets of five antiparallel beta strands that form the walls of a zinc- …

2018年3月30日 · Importantly, we identify the JmjN domain as the KDM4C dimerization interface and pin-point specific charged residues therein to be essential for this dimerization.