2015年6月1日 · Structural studies give insight into how demethylases selectively recognise targets. Specific amino acids, methylation status and context are uniquely recognised. The Jmj catalytic domain, ‘helper’ domains and dimerisation all confer selectivity. The JmjN domain is shown to be an integral core of all KDM catalytic domains.

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.

2010年8月6日 · Histone lysine methylation is a dynamic process that plays an important role in regulating chromatin structure and gene expression. 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.

2006年5月19日 · Histone demethylases, members of a newly emerging transcription-factor family, remove methyl groups from the lysine residues of the histone tails and thereby regulate the transcriptional activity of target genes. JmjC-domain-containing proteins have been predicted to be demethylases.

This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein containing a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers.

2011年9月1日 · 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.

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.

2018年3月30日 · Using size exclusion HPLC as well as Western blot analysis, we show that endogenous KDM4C undergoes dimerization under physiological conditions. Importantly, we identify the JmjN domain as the KDM4C dimerization interface and pin-point specific charged residues therein to be essential for this dimerization.

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.

Here, we highlight the roles of jmj and jumonji family proteins in chromatin regulation and development. The jumonji (jmj) gene was identified by a mouse gene trap approach and has essential roles in the development of multiple tissues. The Jmj protein has a DNA binding domain, ARID, and two conserved jmj domains (jmjN and jmjC).