Extended Data Fig. 6: Course of polypeptide chains of architectural subunits Sth1, Rsc8 and Rsc58 and ATPase–nucleosome interactions.

a, Back view of RSC. The Sth1 subunit of RSC starts with its N terminus in the body module and tracks through it, turning around with a contact helix and loop. Forming the central helix I, the hook and the central helix II it folds back and forth tightly interweaving the body module before it exits with its HSA region through the ARP module to build the ATPase module. b, RSC with the domains of the two Rsc8 subunits highlighted in blue. Both Rsc8 start N-terminal with their SWIRM domains in the arm module where they support the two repeat domains of Sfh1 in a similar manner. They then follow distinct paths through the arm towards the body module where they contribute with both their SANT and ZZ zinc-finger domains. Here the two domains of each subunit form different contacts with various interactions partners and whereas one ZZ zinc-finger ___domain is tightly packed at the body and DNA-interaction module interface, the other seems to extend from the body, presumably as additional interaction surface. Both Rsc8 subunits unite again with their C-terminal long helices in a coiled-coil fold on the opposite side of the body module. c, Rsc58 N-terminal bromodomain attaches to the top of the body module. Then, Rsc58 follows an interwound path through the body module via the central and connector loop. It turns back, docking to the body with a three-helix bundle and stabilizing the module with its C-terminal end. d, Contacts of Sth1 ATPase motor (orange) with the nucleosome. View as in Fig. 1c, left, but rotated by 45° around a horizontal axis. Arrows indicate directionality of DNA translocation.