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The nucleosome acidic patch and H2A ubiquitination underlie mSWI/SNF recruitment in synovial sarcomaMcBride, Matthew J; Mashtalir, Nazar; Winter, Evan B; Dao, Hai T; Filipovski, Martin; D'Avino, Andrew R; Seo, Hyuk-Soo; Umbreit, Neil T; St Pierre, Roodolph; Valencia, Alfredo M; Qian, Kristin; Zullow, Hayley J; Jaffe, Jacob D; Dhe-Paganon, Sirano; Muir, Tom W; Kadoch, Cigall
Nature structural & molecular biology, 09/2020, Letnik: 27, Številka: 9Journal Article
Interactions between chromatin-associated proteins and the histone landscape play major roles in dictating genome topology and gene expression. Cancer-specific fusion oncoproteins, which display unique chromatin localization patterns, often lack classical DNA-binding domains, presenting challenges in identifying mechanisms governing their site-specific chromatin targeting and function. Here we identify a minimal region of the human SS18-SSX fusion oncoprotein (the hallmark driver of synovial sarcoma) that mediates a direct interaction between the mSWI/SNF complex and the nucleosome acidic patch. This binding results in altered mSWI/SNF composition and nucleosome engagement, driving cancer-specific mSWI/SNF complex targeting and gene expression. Furthermore, the C-terminal region of SSX confers preferential affinity to repressed, H2AK119Ub-marked nucleosomes, underlying the selective targeting to polycomb-marked genomic regions and synovial sarcoma-specific dependency on PRC1 function. Together, our results describe a functional interplay between a key nucleosome binding hub and a histone modification that underlies the disease-specific recruitment of a major chromatin remodeling complex.
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