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. 2022 May 17;29(5):493–501. doi: 10.1038/s41594-022-00768-w

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© The Author(s) 2022

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Fig. 3 — a, H1 binds to nucleosomes of the array near the nucleosome dyad. The N-terminal part of the α2-helix (Nα2) and the L3 loop contact the DNA around the dyad, whereas the α3-helix and the L1 loop interact with linker DNAs. H1 is rainbow-colored from the N (blue) to C (red) terminus, DNA is shown in white, and the histone octamer is shown in wheat. b, Focused-refined cryo-EM densities for nucleosomes 1, 2, 3 and 4, colored by NRL (4×177 blue, 4×187 green, 4×197 yellow, 4×207 red). H1 density is in purple. Nucleosomes are all viewed the same way. Entry and exit DNA are marked by a blue and a red dot, respectively. Focused-refined maps of nucleosome 4 could not be obtained for the 4×197 and 4×207 arrays owing to higher mobility. c. H1 N-terminal regions extend from the nucleosome stack in opposite directions. Residues regulating H1 mobility (K34 (ref. ³⁴) and S35 (ref. ³⁵)) and heterochromatin formation (K26 and S27)³⁶ protrude from the nucleosome stack on both sides and are accessible for protein-protein interactions. The first ordered residue of H1 is S35; disordered residues are shown as a dashed line. DNA is shown in gray, histone octamer in wheat and H1 in purple.