Non-histone protein acetylation by the evolutionarily conserved GCN5 and PCAF acetyltransferases

GCN5, conserved from yeast to humans, and the vertebrate specific PCAF, are lysine acetyltransferase enzymes found in large protein complexes. Both enzymes have well documented roles in the histone acetylation and the concomitant regulation of transcription. However, these enzymes also acetylate non-histone substrates to impact diverse aspects of cell physiology. Here, I review our current understanding of non-histone acetylation by GCN5 and PCAF across eukaryotes, from target identification to molecular mechanism and regulation. I focus mainly on budding yeast, where Gcn5 was first discovered, and mammalian systems, where the bulk of non-histone substrates have been characterized. I end the review by defining critical caveats and open questions that apply to all models.

Automated summary

GCN5 and PCAF are lysine acetyltransferase enzymes that play important roles in histone acetylation and non-histone substrate acetylation in eukaryotes. This review focuses on the current understanding of non-histone acetylation by GCN5 and PCAF in budding yeast and mammalian systems, highlighting the diverse impact on cell physiology. Critical caveats and open questions are defined at the end of the review for all models.