Fig. 6: Sth1 bromodomain has Kbz binding activity.
From: Global profiling of regulatory elements in the histone benzoylation pathway
a ITC analyses of four yeast bromodomains binding with H3K14bz peptides. Sth1BD exhibits a detectable interaction with the H3K14bz peptide (Kd = 89 μM). b Superimposition of Sth1BD-H3K14bz (Sth1:orange; H3, cyan) and Sth1BD-H3K14ac (Sth1: yellow; H3, purple) complexes shows almost identical conformations of Sth1BD and H3 peptide, except for the C-terminal 310-helix of H3. c Detailed interaction networks between acylated lysine and Sth1BD. Benzoyl and acetyl groups are shown in cyan and purple, respectively. Hydrophobic contacts and hydrogen-bonding networks are shown. d ITC assays showing the effects of Sth1 mutations on the interaction between Sth1BD and H3K14bz peptide.
