[HTML][HTML] Histone methyltransferase activity of a Drosophila Polycomb group repressor complex

J Müller, CM Hart, NJ Francis, ML Vargas, A Sengupta… - Cell, 2002 - cell.com
J Müller, CM Hart, NJ Francis, ML Vargas, A Sengupta, B Wild, EL Miller, MB O'Connor
Cell, 2002cell.com
Polycomb group (PcG) proteins maintain transcriptional repression during development,
likely by creating repressive chromatin states. The Extra Sex Combs (ESC) and Enhancer of
Zeste [E (Z)] proteins are partners in an essential PcG complex, but its full composition and
biochemical activities are not known. A SET domain in E (Z) suggests this complex might
methylate histones. We purified an ESC-E (Z) complex from Drosophila embryos and found
four major subunits: ESC, E (Z), NURF-55, and the PcG repressor, SU (Z) 12. A recombinant …
Abstract
Polycomb group (PcG) proteins maintain transcriptional repression during development, likely by creating repressive chromatin states. The Extra Sex Combs (ESC) and Enhancer of Zeste [E(Z)] proteins are partners in an essential PcG complex, but its full composition and biochemical activities are not known. A SET domain in E(Z) suggests this complex might methylate histones. We purified an ESC-E(Z) complex from Drosophila embryos and found four major subunits: ESC, E(Z), NURF-55, and the PcG repressor, SU(Z)12. A recombinant complex reconstituted from these four subunits methylates lysine-27 of histone H3. Mutations in the E(Z) SET domain disrupt methyltransferase activity in vitro and HOX gene repression in vivo. These results identify E(Z) as a PcG protein with enzymatic activity and implicate histone methylation in PcG-mediated silencing.
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