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...
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Veröffentlicht in: | Biochimica et biophysica acta. Gene regulatory mechanisms 2021-02, Vol.1864 (2), p.194608-194608, Article 194608 |
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Sprache: | eng |
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Zusammenfassung: | 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.
•A broad role for GCN5 in non-histone acetylation is conserved across eukaryotes.•Hundreds of GCN5 and/or PCAF targets have been investigated in human cells.•Acetylation impacts protein function via diverse mechanisms.•GCN5 and PCAF targeting of non-histone substrates is regulated at multiple levels.•Stoichiometry of acetylation and other acyl-modifications is a key area of research. |
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ISSN: | 1874-9399 1876-4320 |
DOI: | 10.1016/j.bbagrm.2020.194608 |