TY - JOUR T1 - The <em>Drosophila</em> Polycomb Protein Interacts with Nucleosomal Core Particles In Vitro via Its Repression Domain JF - Molecular and Cellular Biology JO - Mol. Cell. Biol. SP - 8451 LP - 8460 DO - 10.1128/MCB.19.12.8451 VL - 19 IS - 12 AU - Breiling, Achim AU - Bonte, Edgar AU - Ferrari, Simona AU - Becker, Peter B. AU - Paro, Renato Y1 - 1999/12/01 UR - http://mcb.asm.org/content/19/12/8451.abstract N2 - The proteins of the Polycomb group (PcG) are required for maintaining regulator genes, such as the homeotic selectors, stably and heritably repressed in appropriate developmental domains. It has been suggested that PcG proteins silence genes by creating higher-order chromatin structures at their chromosomal targets, thus preventing the interaction of components of the transcriptional machinery with theircis-regulatory elements. An unresolved issue is how higher order-structures are anchored at the chromatin base, the nucleosomal fiber. Here we show a direct biochemical interaction of a PcG protein—the Polycomb (PC) protein—with nucleosomal core particles in vitro. The main nucleosome-binding domain coincides with a region in the C-terminal part of PC previously identified as the repression domain. Our results suggest that PC, by binding to the core particle, recruits other PcG proteins to chromatin. This interaction could provide a key step in the establishment or regulation of higher-order chromatin structures. ER -