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Cell. 2015 Jan 15;160(1-2):204-18. doi: 10.1016/j.cell.2014.11.039. Epub 2014 Dec 18.

Product binding enforces the genomic specificity of a yeast polycomb repressive complex.

Author information

  • 1Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
  • 2Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • 3Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.
  • 4Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
  • 5Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: hitenmadhani@gmail.com.

Abstract

We characterize the Polycomb system that assembles repressive subtelomeric domains of H3K27 methylation (H3K27me) in the yeast Cryptococcus neoformans. Purification of this PRC2-like protein complex reveals orthologs of animal PRC2 components as well as a chromodomain-containing subunit, Ccc1, which recognizes H3K27me. Whereas removal of either the EZH or EED ortholog eliminates H3K27me, disruption of mark recognition by Ccc1 causes H3K27me to redistribute. Strikingly, the resulting pattern of H3K27me coincides with domains of heterochromatin marked by H3K9me. Indeed, additional removal of the C. neoformans H3K9 methyltransferase Clr4 results in loss of both H3K9me and the redistributed H3K27me marks. These findings indicate that the anchoring of a chromatin-modifying complex to its product suppresses its attraction to a different chromatin type, explaining how enzymes that act on histones, which often harbor product recognition modules, may deposit distinct chromatin domains despite sharing a highly abundant and largely identical substrate-the nucleosome.

PMID:
25533783
PMCID:
PMC4303595
DOI:
10.1016/j.cell.2014.11.039
[PubMed - indexed for MEDLINE]
Free PMC Article
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