Extended Data Fig. 6: Histone tails deacetylated by Rpd3S.
From: Structure of histone deacetylase complex Rpd3S bound to nucleosome
a, The density of histone peptide bound to Rpd3S. Two possible histone H3 tail fragments could be assigned to this density. H3 residues 8–20 was assigned according to the continuity of the density from the H3 N-terminus bound to the Rco1 PHD1 towards the active site of Rpd3 (upper). Alternatively, H3 residues 13–25 was assigned based on the register of bulky side chains (low). b, H3K9 is unreachable to the active site of Rpd3. The distance from K9 residue to the active site of Rpd3 is 15 Å which is too large for the coiled linker (T6-R8) to span. c, The H4 tail is close to the Rpd3S active site. The N-terminal tail of H4 is just beneath the active site of Rpd3S with a distance of 30 Å from the resolved terminal residue of H4 to the lysine in the catalytic pocket in the structure. d, Rpd3S binds to the nucleosome to release the unspecific attachment of H4. The H4 tail may attach to nucleosomal DNA. Binding of Rpd3S at SHL –2 may drive the H4 towards the active site.
