Department of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, Georgia.
Curr Protoc. 2023 Apr;3(4):e746. doi: 10.1002/cpz1.746.
Protein posttranslational modification (PTM) is a biochemical mechanism benefitting cellular adaptation to dynamic intracellular and environmental conditions. Recently, several acylation marks have been identified as new protein PTMs occurring on specific lysine residues in mammalian cells: isobutyrylation, methacrylation, benzoylation, isonicotinylation, and lactylation. These acylation marks were initially discovered to occur on nucleosomal histones, but they potentially occur as prevalent biomarkers on non-histone proteins as well. The existence of these PTMs is a downstream consequence of metabolism and demonstrates the intimate crosstalk between active cellular metabolites and regulation of protein function. Emerging evidence indicates that these acylation marks on histones affect DNA transcription and are functionally distinct from the well-studied lysine acetylation. Herein, we discuss enzymatic regulation and metabolic etiology of these acylations, 'reader' proteins that recognize different acylations, and their possible physiological and pathological functions. Several of these modifications correlate with other well-studied acylations and fine-tune the regulation of gene expression. Overall, findings of these acylation marks reveal new molecular links between metabolism and epigenetics and open up many questions for future investigation. © 2023 The Authors. Current Protocols published by Wiley Periodicals LLC.
蛋白质翻译后修饰（PTM）是一种生化机制，有助于细胞适应动态的细胞内和环境条件。最近，已经确定了几种酰化标记作为哺乳动物细胞中特定赖氨酸残基上的新蛋白质 PTM：异丁酰化、甲基丙烯酰化、苯甲酰化、异烟酰化和乳酰化。这些酰化标记最初是在核小体组蛋白上发现的，但它们也可能作为非组蛋白蛋白质上的常见生物标志物存在。这些 PTM 的存在是代谢的下游结果，表明活性细胞代谢物与蛋白质功能调节之间的密切相互作用。新出现的证据表明，这些组蛋白上的酰化标记影响 DNA 转录，并且与研究充分的赖氨酸乙酰化在功能上不同。本文讨论了这些酰化的酶调节和代谢病因、识别不同酰化的“读取器”蛋白及其可能的生理和病理功能。其中一些修饰与其他研究充分的酰化相关，微调基因表达的调节。总的来说，这些酰化标记的发现揭示了代谢和表观遗传学之间的新分子联系，并为未来的研究提出了许多问题。© 2023 作者。Wiley Periodicals LLC 出版的《当代方案》。
