Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-12, Nishi-6, Kita-ku, Sapporo 060-0812, Japan.
Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-12, Nishi-6, Kita-ku, Sapporo 060-0812, Japan.
Chem Asian J. 2022 Jul 1;17(13):e202200197. doi: 10.1002/asia.202200197. Epub 2022 May 18.
Post-translational modifications (PTMs) of histones play a key role in epigenetic regulation. Unraveling the roles of each epigenetic mark can provide new insights into their biological mechanisms. On the other hand, it is generally difficult to prepare homogeneously-modified histones/nucleosomes to investigate their specific functions. Therefore, synthetic approaches to acquire precisely mimicked histones/nucleosomes are in great demand, and further development of this research field is anticipated. In this review, synthetic strategies to modify histones/nucleosomes, including cysteine modifications, transformations of dehydroalanine residues and lysine acylation using a catalyst system, are cited. In addition, the functional evaluation of synthetically modified histones/nucleosomes is described.
组蛋白的翻译后修饰（PTMs）在表观遗传调控中起着关键作用。揭示每个表观遗传标记的作用可以为它们的生物学机制提供新的见解。另一方面，通常很难制备均匀修饰的组蛋白/核小体来研究它们的特定功能。因此，人们迫切需要采用合成方法获得精确模拟的组蛋白/核小体，预计这一研究领域将会进一步发展。在这篇综述中，引用了修饰组蛋白/核小体的合成策略，包括半胱氨酸修饰、使用催化剂系统转化脱氢丙氨酸残基和赖氨酸酰化。此外，还描述了合成修饰的组蛋白/核小体的功能评价。
