Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity

Elias Seif, Jin Joo Kang, Charles Sasseville, Olga Senkovich, Alexander Kaltashov, Elodie L. Boulier, Ibani Kapur, Chongwoo A. Kim and Nicole J. Francis ()
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Elias Seif: Institut de recherches cliniques de Montréal
Jin Joo Kang: Institut de recherches cliniques de Montréal
Charles Sasseville: Institut de recherches cliniques de Montréal
Olga Senkovich: Midwestern University
Alexander Kaltashov: Institut de recherches cliniques de Montréal
Elodie L. Boulier: Institut de recherches cliniques de Montréal
Ibani Kapur: Institut de recherches cliniques de Montréal
Chongwoo A. Kim: Midwestern University
Nicole J. Francis: Institut de recherches cliniques de Montréal

Nature Communications, 2020, vol. 11, issue 1, 1-19

Abstract: Abstract Polycomb Group (PcG) proteins organize chromatin at multiple scales to regulate gene expression. A conserved Sterile Alpha Motif (SAM) in the Polycomb Repressive Complex 1 (PRC1) subunit Polyhomeotic (Ph) has been shown to play an important role in chromatin compaction and large-scale chromatin organization. Ph SAM forms helical head to tail polymers, and SAM-SAM interactions between chromatin-bound Ph/PRC1 are believed to compact chromatin and mediate long-range interactions. To understand the underlying mechanism, here we analyze the effects of Ph SAM on chromatin in vitro. We find that incubation of chromatin or DNA with a truncated Ph protein containing the SAM results in formation of concentrated, phase-separated condensates. Ph SAM-dependent condensates can recruit PRC1 from extracts and enhance PRC1 ubiquitin ligase activity towards histone H2A. We show that overexpression of Ph with an intact SAM increases ubiquitylated H2A in cells. Thus, SAM-induced phase separation, in the context of Ph, can mediate large-scale compaction of chromatin into biochemical compartments that facilitate histone modification.

Date: 2020
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DOI: 10.1038/s41467-020-19435-z

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