Glycine max JmjC domain-containing proteins JMJ19/20 exhibit endopeptidase activity and interact with LUXs to mediate flowering time

However, their roles in Glycine max remain largely unexplored. This study identified GmJMJ19 and GmJMJ20, encoding JmjC domain-containing proteins.

They exhibit circadian rhythmic expression patterns and interact with LUX ARRHYTHMO 2 (GmLUX2) both in vitro and in vivo. Although GmJMJ19/20 bind to histones, they lack conventional histone demethylase activity. Rather, GmJMJ19/20 function as endopeptidases that specifically cleave histone H3 peptides at unmethylated lysine 27 residues, in a manner independent of Fe²⁺ and α-ketoglutarate (α-KG), the cofactors required for typical JmjC enzymes.