Abstract
A heterotrimeric SMARCB1\u2013SMARCC2 subcomplex is required for the assembly and tumor suppression function of the BAF chromatin-remodeling complex
Highlights
1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; Dear Editor, The SWI/SNF complex utilizes its ATP-dependent chromatin-remodeling activity to mobilize nucleosomes and regulates DNA accessibility at nucleosomal templates
We found that a region of SMARCB1 (aa 169–385, SMARCB1(169–385)), and the SWIRM domain of SMARCC2 (aa 423–518, SMARCC2(423–518)) (Fig. 1a) form a stable subcomplex (Supplementary Fig. S1g)
As anticipated from the structure, biochemical assays indicated that R487C or R512Q reduces the interaction of SMARCC2 or SMARCC1 with SMARCB1, respectively (Supplementary Fig. S7c-f)
Summary
1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; Dear Editor, The SWI/SNF complex utilizes its ATP-dependent chromatin-remodeling activity to mobilize nucleosomes and regulates DNA accessibility at nucleosomal templates. Each Rpt motif-mediated complex structure of the SMARCB1Rpt1Rpt2/SMARCC2SWIRM heterotrimeric subcomplex determined in our manuscript is similar to the corresponding portion of the SMARCB1/SMARCC2 subcomplex from the holo-BAF complex (Supplementary Fig. S4). The Rpt[1] and Rpt[2] motifs of SMARCB1 bind to the SWIRM domains of two distinct SMARCC2 molecules, promoting the formation a tripartite complex.
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