Yang Xiang-Jiao, Grégoire Serge
Molecular Oncology Group, Department of Medicine, Royal Victoria Hospital, Room H5.41, McGill University Health Centre, 687 Pine Avenue West, Montréal, Québec H3A 1A1, Canada.
EMBO Rep. 2007 Jun;8(6):556-62. doi: 10.1038/sj.embor.7400977.
Acetylation of the epsilon-amino group of lysine residues (N(epsilon)-acetylation) is a reversible post-translational modification with the potential to rival phosphorylation. In addition to histones and many transcription factors such as p53, regulators of DNA repair, replication and recombination are subject to N(epsilon)-acetylation. This modification is also important for governing the activities of various enzymes, including histone acetyltransferases, histone deacetylases, bacterial and mammalian acetyl-CoA synthases, kinases, phosphatases, the ubiquitin ligase murine double minute 2 and the chaperonin heat shock protein 90. Furthermore, lysine acetylation occurs in cellular structure proteins such as alpha-tubulin, actin, cortactin and p120 catenin. Strikingly, the Yersinia outer protein YopJ promotes O-acetylation of crucial serine and threonine residues that are required for activation of the MAPK/ERK kinase and IkappaB kinase families, which precludes their phosphorylation and blocks signal transduction. Thus, N(epsilon)- and O-acetylation are becoming recognized as two prominent mechanisms for regulating protein functions in diverse organisms.
赖氨酸残基的ε-氨基乙酰化（N（ε）-乙酰化）是一种可逆的翻译后修饰，其作用潜力可与磷酸化相媲美。除了组蛋白和许多转录因子（如p53）外，DNA修复、复制和重组的调节因子也会发生N（ε）-乙酰化。这种修饰对于调控各种酶的活性也很重要，这些酶包括组蛋白乙酰转移酶、组蛋白去乙酰化酶、细菌和哺乳动物的乙酰辅酶A合成酶、激酶、磷酸酶、泛素连接酶小鼠双微体2和伴侣蛋白热休克蛋白90。此外，赖氨酸乙酰化还发生在细胞结构蛋白中，如α-微管蛋白、肌动蛋白、皮层肌动蛋白和p120连环蛋白。引人注目的是，耶尔森氏菌外蛋白YopJ可促进丝裂原活化蛋白激酶/细胞外信号调节激酶（MAPK/ERK）激酶家族和IkappaB激酶家族激活所需的关键丝氨酸和苏氨酸残基的O-乙酰化，从而阻止它们的磷酸化并阻断信号转导。因此，N（ε）-乙酰化和O-乙酰化正逐渐被认为是调节多种生物体中蛋白质功能的两种重要机制。
