Histone H2B ubiquitylation represses gametogenesis by opposing RSC-dependent chromatin remodeling at the ste11 master regulator locus. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Genome-wide reconstitution of chromatin transactions reveals that RSC preferentially disrupts H2AZ-containing nucleosomes. Histone acetylation inhibits RSC and stabilizes the +1 nucleosome. The SnAC domain of SWI/SNF is a histone anchor required for remodeling.
The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases. Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler. Chromatin remodeling through directional DNA translocation from an internal nucleosomal site.
Mechanism of DNA translocation underlying chromatin remodelling by Snf2. Autoregulation of the Rsc4 tandem bromodomain by Gcn5 acetylation. Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14. The BAH domain of Rsc2 is a histone H3 binding domain. Composition and function of mammalian SWI/SNF chromatin remodeling complexes in human disease. Sequence-directed action of RSC remodeler and general regulatory factors modulates +1 nucleosome position to facilitate transcription. Role of DNA sequence in chromatin remodeling and the formation of nucleosome-free regions. A library of yeast transcription factor motifs reveals a widespread function for Rsc3 in targeting nucleosome exclusion at promoters. Asymmetric nucleosomes flank promoters in the budding yeast genome.
Nucleosome stability distinguishes two different promoter types at all protein-coding genes in yeast. Dynamics of chromatin and transcription during transient depletion of the RSC chromatin remodeling complex. Klein-Brill, A., Joseph-Strauss, D., Appleboim, A. Genomic nucleosome organization reconstituted with pure proteins. Regulation of DNA translocation efficiency within the chromatin remodeler RSC/Sth1 potentiates nucleosome sliding and ejection. Chromatin remodeling by RSC involves ATP-dependent DNA translocation. RSC, an essential, abundant chromatin-remodeling complex. Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes. The RSC–nucleosome structure provides a basis for understanding NDR formation and the structure and function of human SWI/SNF complexes that are frequently mutated in cancer 13. The mobile ARP module may modulate translocase–nucleosome interactions to regulate RSC activity 5. The translocase motor of the ATPase module engages with the edge of the nucleosome at superhelical location +2. The ATPase and arm modules sandwich the nucleosome disc with the Snf2 ATP-coupling (SnAC) domain and the finger helix, respectively. The DNA-interacting module binds extra-nucleosomal DNA and is involved in the recognition of promoter DNA elements 8, 10, 11 that influence RSC functionality 12. The body module serves as a scaffold for the four flexible modules that we call DNA-interacting, ATPase, arm and actin-related protein (ARP) modules. The structure reveals that RSC forms five protein modules and suggests key features of the remodelling mechanism. Here we present the cryo-electron microscopy structure of RSC in complex with a nucleosome substrate. RSC removes nucleosomes from promoter regions 6, 7 and positions the specialized +1 and −1 nucleosomes that flank NDRs 8, 9. In the yeast Saccharomyces cerevisiae, the essential SWI/SNF complex RSC 3 contains 16 subunits, including the ATP-dependent DNA translocase Sth1 4, 5. Chromatin-remodelling complexes of the SWI/SNF family function in the formation of nucleosome-depleted, transcriptionally active promoter regions (NDRs) 1, 2.