Abstract
The faithful inheritance of the gene expression program requires not only modifications to DNA and histones but also reestablishment of the three-dimensional state of chromatin. The forces that underlie assembly of these states are the collection of noncovalent interaction modules present in all epigenetic regulatory proteins. The focus here is on two protein interaction domains, the RING finger and WD40-associated ubiquitin-like (RAWUL) and Sterile Alpha Motif (SAM), which function within the multiprotein assembly called Polycomb repression complex 1 (PRC1) and are instrumental in creating the precise three-dimensional state of chromatin. Structural studies of the RAWUL have revealed the key role it plays in forming functionally distinct variations of PRC1. SAM, which has a unique ability to form polymers, has emerged as a key player in the clustering of gene elements required to form repressed chromatin architectures.
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