Histone methyltransferase activity of a Drosophila Polycomb group repressor complex

Jürg Müller, Craig M. Hart, Nicole J. Francis, Marcus L. Vargas, Aditya Sengupta, Brigitte Wild, Ellen L. Miller, Michael B. O'Connor, Robert E. Kingston, Jeffrey A. Simon

Research output: Contribution to journalArticle

1076 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)197-208
Number of pages12
JournalCell
Volume111
Issue number2
DOIs
StatePublished - Oct 18 2002

Fingerprint Dive into the research topics of 'Histone methyltransferase activity of a Drosophila Polycomb group repressor complex'. Together they form a unique fingerprint.

  • Cite this

    Müller, J., Hart, C. M., Francis, N. J., Vargas, M. L., Sengupta, A., Wild, B., Miller, E. L., O'Connor, M. B., Kingston, R. E., & Simon, J. A. (2002). Histone methyltransferase activity of a Drosophila Polycomb group repressor complex. Cell, 111(2), 197-208. https://doi.org/10.1016/S0092-8674(02)00976-5