Fig. 3
From: Structure and function of the Orc1 BAH-nucleosome complex
Orc1 does not discriminate the acetylation state of H4K16. a Binding of Orc1 BAH domain (Orc1) to unmodified (WT nuc) and H4K16ac nucleosomes measured by EMSA. b Binding of Sir3 D205N BAH domain to unmodified and H4K16ac nucleosomes measured by EMSA. c Sequence alignment of variable Loop 2 region in Orc1 and Sir3. Loop 2 Lid residues are highlighted in a box. Asterisk represents a dominant loss of silencing mutation in Sir3. d Binding of Orc1 with Sir3-swapped residues in the Lid of Loop 2 to unmodified or H4K16Q (acetyl mimic) nucleosomes measured by EMSA. e Binding of Orc1 with Sir3-swapped residues in the Lid of Loop 2 to unmodified and H4K16ac nucleosomes measured by EMSA shows that these residues confer discrimination for H4K16. Each data point and error bar represent the mean ± s.d. from three or more independent experiments. The standard errors of dissociation constants (KD) are indicated
