Jumonji
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Related Articles from SNS
Histone succinylation directly inhibits Jumonji domain demethylases and stabilizes repressive chromatin states
Herein we uncover a relationship between histone succinylation and Jumonji (JmjC) domain-containing histone demethylases. We used quantitative proteomics and peptide pull-down assays to identify JmjC demethylases as candidate interactors with succinylated histone peptides. Succinyl-lysine peptides bind and inhibit the catalytic activity of JmjC demethylases in a dose-dependent manner.
Quantitative profiling of JMJD6-catalysed lysine hydroxylation reveals residue-dependent oxygen sensitivity
Lysine hydroxylation is increasingly recognised as a widespread post-translational modification in human cells, with more than 100 modified sites identified to date. Jumonji domain-containing protein 6 (JMJD6) catalyses hydroxylation at multiple lysines within lysine-rich regions and is a major contributor to this modification across the proteome. As JMJD6 requires oxygen as a co-substrate, lysine hydroxylation has been proposed to couple oxygen availability to cellular function.