DESCRIPTION:Human recombinant SUV420H1, transcript variant 1 expressed in Sf9 insect cells with an N-terminal GST-tag. Catalyzes the transfer of methyl groups from S-adenosyl-L-methionine (SAM) to the epsilon-amino function of protein L-lysine residues, specifically converting monomethyl histone H4 lysine-20 (H4K20me) to the di- and trimethylated forms (H4K20me2/3). Results with mice and mouse cells deleted of SUV420H1 and/or the related enzyme SUV420H2 suggest that, in vivo, SUV420H1 may have the primary role in generating H4K20me2, whereas H4K20me3 is mostly the product of SUV420H2. However, transfection and chromatin localization studies with the human enzymes SUV420H1-tv1, SUV420H1-tv2 and SUV420H2 implicate all three in the generation of H4K20me3, with SUV420H1-tv1 and SUV420H2 targeted to pericentric heterochromatin. The methylation state of H4K20 is linked to the cell cycle, with the SUV420H1 conversion of SET8-generated H4K20me1 to H4K20me2 occurring broadly throughout the genome in the G1 phase. Entry into S-phase is delayed by an SUV420H1/2 double knockout, presumably due to the role of these enzymes and H4K20me2/3 in recruitment of the origin of replication complex (ORC). The SUV420H enzymes also play a role in DNA damage repair via the stabilizing effect of H4K20me2 on recruitment of 53BP1 to double strand breaks. The decrease in H4K20me3 at telomeres in SUV420H1/2-depleted cells promotes telomere elongation and recombination. Induced pluripotent stem cells (iPS) generated from SUV420H1/2-deleted cells display both these telomere effects and increased tumorigenic potential, suggesting, along with the prevalent loss of H4K20me3 from human cancer cells, that SUV420H1/2 may function as tumor suppressors.

SUPPLIED AS: Solution of purified recombinant protein in 50 mM Tris/HCl pH 7.5, 500 mM NaCl, 1 mM TCEP, 10% glycerol (v/v).

STORAGE: -80°C, aliquot and snap-freeze after first use.

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