Constantinou Mamantia, Klavaris Ariel, Koufaris Costas, Kirmizis Antonis
Epigenetics and Gene Regulation Laboratory, Department of Biological Sciences, University of Cyprus, 2109 Nicosia, Cyprus.
J Cell Sci. 2023 Apr 1;136(7). doi: 10.1242/jcs.260801. Epub 2023 Apr 4.
Histone acetylation involves the addition of acetyl groups to specific amino acid residues. This chemical histone modification is broadly divided into two types - acetylation of the amino group found on the side chain of internal lysine residues (lysine acetylation) or acetylation of the α-amino group at the N-terminal amino acid residue (N-terminal acetylation). Although the former modification is considered a classic epigenetic mark, the biological importance of N-terminal acetylation has been mostly overlooked in the past, despite its widespread occurrence and evolutionary conservation. However, recent studies have now conclusively demonstrated that histone N-terminal acetylation impacts important cellular processes, such as controlling gene expression and chromatin function, and thus ultimately affecting biological phenotypes, such as cellular ageing, metabolic rewiring and cancer. In this Review, we provide a summary of the literature, highlighting current knowledge on the function of this modification, as well as allude to open questions we expect to be the focus of future research on histone N-terminal acetylation.
组蛋白乙酰化涉及将乙酰基添加到特定氨基酸残基上。这种化学性组蛋白修饰大致可分为两类——内部赖氨酸残基侧链上氨基的乙酰化（赖氨酸乙酰化）或N端氨基酸残基处α-氨基的乙酰化（N端乙酰化）。尽管前一种修饰被认为是经典的表观遗传标记，但过去N端乙酰化的生物学重要性大多被忽视，尽管它广泛存在且具有进化保守性。然而，最近的研究现已确凿地证明，组蛋白N端乙酰化会影响重要的细胞过程，如控制基因表达和染色质功能，从而最终影响生物学表型，如细胞衰老、代谢重塑和癌症。在这篇综述中，我们对文献进行了总结，突出了关于这种修饰功能的当前知识，并提及了我们预期将成为未来组蛋白N端乙酰化研究重点的未解决问题。
