Fig. 4: CHES1 was acetylated by p300 and deacetylated by HDAC1.

A Endogenous IP assay showed the acetylated CHES1 in the presence of pan-HDACs inhibitors. B CoIP assay showed that CHES1 could be acetylated by p300 but not other acetyltransferases. “*” denotes the non-specific band. C CoIP assay showed the disability of catalytic deficient mutants of p300 on the acetylation of CHES1. D, E CoIP assay showed the endogenous interaction between CHES1 and p300 in TNBC. F IP assay showed the effect of HDACs inhibitors on the acetylation levels of CHES1. G The schematic diagram of the main steps for identifying the acetylation lysine sites of CHES1 by mass spectrometry (MS). H Tandem mass spectrum of the peptide (m/z = 491.59) HNLSLNKCFKK containing acetylated K170 and K173 of CHES1. The “ac” above the Lys indicates an acetyl remnant on this Lys. I The schematic representation of the 21 acetylated lysine sites in the protein domains of CHES1. J CoIP assay showed the acetylation levels of wild type CHES1 and its KR mutant.