The histone acetyltransferase PCAF regulates p21 transcription through stress-induced acetylation of histone H3

p53-dependent growth arrest and induction of p21: A critical role for PCAF-mediated histone acetylation

“…These findings raised the possibility that the critical substrates for PCAF acetylation were in fact the nucleosomal histones bound to the p21 promoter. Indeed, chromatin immunoprecipitation experiments performed by Love et al showed that acetylation of histone H3 K9 and K14 was increased upon p53 activation, an effect that required the presence of enzymatically active PCAF 8 . These two histone H3 residues were previously demonstrated to be the preferred histone substrates of PCAF.…”

“…GNAT family members PCAF and GCN5 primarily acetylate K320 in the nuclear location signal of p53. This modification occurs after DNA damage and contributes to the stabilization of p53 and enhances its ability to bind DNA 2 , 3 , 8 . The third group of HATs, p300 and CBP, modifies several lysine residues in the C terminus, including K373 and K382, and K164 in the DNA binding domain 1 , 3 , 4 .…”

Acetylation promotes TyrRS nuclear translocation to prevent oxidative damage

“…Lysine acetylation is a reversible process catalyzed by acetyltransferases and deacetylases (9). To identify the acetyltransferase responsible for TyrRS acetylation, we overexpressed p300/CBP-associated factor (PCAF), Tip60, and GCN5 into HEK293T cells, because PCAF, Tip60, and GCN5 have been shown to respond to oxidative stress (22)(23)(24)(25), and found that the acetylation of TyrRS was elevated only after the ectopic expression of PCAF, not the other acetyltransferases ( Fig. 2A).…”

Acetylation dynamics of human nuclear proteins during the ionizing radiation-induced DNA damage response

“…For example, the HAT protein p300/CREB-binding protein-associated factor (PCAF) regulates the p53-induced transcription of p21 via acetylation of histone H3 tails. 7 In addition to transcription regulation during the DDR, histone acetylation also plays a role in regulating access for repair factors to chromatin through the actions of the HAT TIP60 and HDACs, including HDAC1 and HDAC2. 8,9 Besides histones, multiple DDR proteins have been shown to be acetylated, and for some of these, the acetylation status was shown to change upon DNA damage induction.…”