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. Author manuscript; available in PMC: 2020 Aug 21.
Published in final edited form as: Nature. 2019 Nov 27;577(7790):426–431. doi: 10.1038/s41586-019-1820-0

Extended Data Figure 8: Interactions between H3-H4 and SPT16 MD (4Z2M) are incompatible with FACT interactions made with the sub-nucleosome.

Extended Data Figure 8:

a. Schematic of SPT16 domain structure, and cartoon of overall complex architecture

b. Interaction between H3-H4 and SPT16 MD (4Z2M) are incompatible with FACT interactions made with the sub-nucleosome. Complex 1 showing only the SPT16 MD. Two sites of interaction with the sub-nucleosome (interface 1: near the H2A docking domain and nearby DNA; interface 2: near H4 N-tail and DNA) are indicated by boxes.

c. The presence of DNA and the H2A-H2B dimer completely occludes interactions between the SPT16 MD and the (H3-H4)2 tetramer in 4Z2M (clash 1 and clash 2, indicated by red arrows).