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Trimethylation on histone H3 lysine 27 (H3K27me3) by Polycomb repressive complex 2 (PRC2) regulates the balance between self-renewal and differentiation of embryonic stem cells (ESCs). The mechanisms by which the activity and recruitment of PRC2 are controlled are largely unknown. Here we demonstrate that the founding member of the Jumonji-family, JMJ (JUMONJI or JARID2), is tightly associated with PRC2, colocalizes with PRC2 and H3K27me3 on chromatin, and modulates PRC2 function. In vitro JMJ inhibits PRC2 methyltransferase activity, a finding consistent with increased H3K27me3 marks at PRC2 targets in Jmj −/− ESCs. Paradoxically, JMJ is required for efficient binding of PRC2, indicating that the interplay of PRC2 and JMJ fine-tunes deposition of the H3K27me3 mark. During differentiation, activation of genes marked by H3K27me3 and lineage commitments are delayed in Jmj −/− ESCs.

Our results demonstrate that dynamic regulation of Polycomb complex activity orchestrated by JMJ balances self-renewal and differentiation, further highlighting the involvement of chromatin dynamics in cell-fate transitions. INTRODUCTION Eukaryotic gene transcription is influenced by chromatin structure, in large part established through modification of histone tails (). Methylation of lysine residues in histones is dynamically regulated by the opposing activities of histone lysine methyltransferases (KMTs) and demethylases (KDMs) (). Recently several KDMs with exquisite substrate specificity have been implicated in diverse processes, including embryonic patterning, stem cell self-renewal, differentiation, neuronal development and spermatogenesis (). Mutations or deregulation of KDMs are often linked to human cancers and diseases (; ).

The majority of KDMs are characterized by the presence of a JmjC domain, a conserved region first recognized in the founding member of the Jumonji family, JUMONJI (JMJ or JARID2). A catalytic triad (H, D/E, H), which is predicted to mediate cofactor Fe(II) binding, is highly conserved in JmjC-containing proteins and required for KDM activity (). JMJ, however, has amino acid substitutions in this subregion, and is predicted to be enzymatically inactive (). Nonetheless, JMJ is critical in embryonic development. The King Of Fighters 2002 Unlimited Match Ps2 Isos.

Jmj −/− mouse embryos develop various defects in neuronal, cardiac, liver and hematopoietic tissues with penetrance dependent on the genetic background (; ). Developmental defects have been associated with increased numbers of progenitor cells and depletion of differentiating or mature cells, suggesting a role for JMJ in regulating proliferation and differentiation. Despite the activities of JMJ-related proteins in chromatin regulation and the multiple roles of JMJ in development, the function of JMJ is poorly understood. Polycomb group (PcG) proteins are required for establishing and maintaining cellular memory. Four PcG proteins, including two EZH proteins (EZH1 / EZH2), EED and SUZ12, comprise the core of the Polycomb repressive complex 2 (PRC2), a methyltransferase complex that acts specifically on histone H3 lysine 27 (H3K27) (; ). In embryonic stem cells (ESCs), PRC2 is critically required for both maintenance and execution of pluripotency (;; ). PRC2 and tri-methylation on H3K27 (H3K27me3) occupy a set of genes controlling differentiation and prevent full expression of these genes until lineage commitment.