Structure of the SWI/SNF complex bound to the nucleosome and insights into the functional modularity

摘要

a Two different views of the cryo-EM density superimposed with the structure of the SWI/SNF–NCP complex, showing the overall modularity (motor-regulation-recruitment) of the complex. Arrows indicate the directions of DNA translocation suggested by the binding position of the motor (Snf2). b Domain organization of the subunits within the SRM. YL-SWIB, the topologically linked YEATS-like and SWIB domain. c Structure of the SRM of the SWI/SNF complex. The proposed position of Taf14 subunit is indicated by the gray oval. The N-termini of Snf5 and Swi1 are labeled. d Structure of the C-terminal tail of Snf5. The boxed region is further analyzed in e. e Binding of the FH of Snf5 to the acidic pocket of H2A–H2B. f Local EM density map of the FH. g Relative ATPase activities of WT (black) and Snf5 mutant (red). Error bars indicate SD of the mean (n = 3 independent experiments). h Nucleosome remodeling activities of WT (black) and Snf5 mutant (red). Error bars indicate SD of the mean (n = 3 independent experiments). i Growth assays of yeast cells with WT and Snf5 mutant. All assays were performed in triplicate, and the representative ones are shown. j Structure of Snf12 (orange) within the NCP-bound SWI/SNF complex (gray). k Structures of the YEATS-like and SWIB domains. Arg126 is marked as a magenta dot. l The Snf12 mutation (G287K) resulted in sodium chloride sensitivity. m The Snf12 mutation (G287K) conferred copper sulfate resistance.