Biomolecules & Therapeutics : eISSN 2005-4483 / pISSN 1976-9148

Download original image
Fig. 2. RBN supplementation inhibited p300 activity through RBN-p300 binding. (A) The WD-induced HAT activity was attenuated following RBN supplementation. HAT activities was measured in nuclear extracts (NEs) derived from mouse livers after 12-week RBN supplementation with WD (n=6/each group). The average OD values are presented as the means ± SE. The means with different superscript letters are significantly different, p<0.05. (B) RBN suppressed p300 activity. Enzyme-specific inhibitory capacity of RBN against p300 was measured using purified recombinant protein. A colorimetric histone acetyltransferase assay was conducted at the indicated concentrations. The results are demonstrated as the relative fold change of the control, and the values presented are the means ± SD of three independent experiments. The means with different superscript letters are significantly different, p<0.05 (one-way ANOVA) (left panel). The IC50 value of RBN inhibition was calculated using the Prism software (right panel). (C) RBN bind mode. Acetyl-transferase domain of p300 and Lys-CoA (PDB ID: 3BIY). (D) The best binding pose of RBN to p300. RBN is presented as yellow sticks, and Lys-CoA is shown as transparent orange sticks. The hydrogen bondings to p300 were represented by blue (for RBN) and red (for Lys-CoA) dashes. (E) The schematic representation of RBN–p300 interaction.
Biomolecules & Therapeutics 2024;32:214~223
© Biomolecules & Therapeutics