Max-Planck-Institute for Terrestrial Microbiology and Center for Synthetic Microbiology, 35043 Marburg, Germany.
Max-Planck-Institute for Terrestrial Microbiology and Center for Synthetic Microbiology, 35043 Marburg, Germany; Center for Synthetic Microbiology (SYNMIKRO), Philipps-Universität Marburg, Marburg, Germany.
Biochim Biophys Acta Mol Cell Res. 2024 Dec;1871(8):119826. doi: 10.1016/j.bbamcr.2024.119826. Epub 2024 Aug 24.
In nature, the majority of known RNA-protein interactions are transient. Our recent study has depicted a novel mechanism known as RNAylation, which covalently links proteins and RNAs. This novel modification bridges the realms of RNA and protein modifications. This review specifically explores RNAylation catalyzed by bacteriophage T4 ADP-ribosyltransferase ModB, with a focus on its protein targets and RNA substrates in the context of Escherichia coli-bacteriophage T4 interaction. Additionally, we discuss the biological significance of RNAylation and present perspectives on RNAylation as a versatile bioconjugation strategy for RNAs and proteins.
在自然界中,大多数已知的 RNA-蛋白质相互作用都是短暂的。我们最近的研究描绘了一种称为 RNAylation 的新机制,它将蛋白质和 RNA 共价连接。这种新的修饰将 RNA 和蛋白质修饰的领域联系起来。本综述特别探讨了由噬菌体 T4 ADP-ribosyltransferase ModB 催化的 RNAylation,重点介绍了在大肠杆菌-噬菌体 T4 相互作用背景下的蛋白质靶标和 RNA 底物。此外,我们还讨论了 RNAylation 的生物学意义,并提出了将 RNAylation 作为 RNA 和蛋白质的通用生物偶联策略的观点。