Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 6038555, Japan.
Faculty of Sciences, Japan Women's University, Tokyo 1120015, Japan.
Toxins (Basel). 2024 Jul 11;16(7):313. doi: 10.3390/toxins16070313.
ADP-ribosylation is a ubiquitous modification of proteins and other targets, such as nucleic acids, that regulates various cellular functions in all kingdoms of life. Furthermore, these ADP-ribosyltransferases (ARTs) modify a variety of substrates and atoms. It has been almost 60 years since ADP-ribosylation was discovered. Various ART structures have been revealed with cofactors (NAD or NAD analog). However, we still do not know the molecular mechanisms of ART. It needs to be better understood how ART specifies the target amino acids or bases. For this purpose, more information is needed about the tripartite complex structures of ART, the cofactors, and the substrates. The tripartite complex is essential to understand the mechanism of ADP-ribosyltransferase. This review updates the general ADP-ribosylation mechanism based on ART tripartite complex structures.
ADP-核糖基化是一种普遍存在的蛋白质和其他靶标（如核酸）修饰方式，可调节所有生命领域的各种细胞功能。此外，这些 ADP-核糖基转移酶（ARTs）修饰各种底物和原子。自 ADP-核糖基化被发现以来，已经过去了近 60 年。已经揭示了具有辅助因子（NAD 或 NAD 类似物）的各种 ART 结构。然而，我们仍然不知道 ART 的分子机制。需要更好地了解 ART 如何指定靶氨基酸或碱基。为此，需要更多关于 ART、辅助因子和底物的三分复合体结构的信息。三分复合体对于理解 ADP-核糖基转移酶的机制至关重要。本综述根据 ART 三分复合体结构更新了通用的 ADP-核糖基化机制。
