Environmental Toxicology Graduate Program, University of California, Riverside, United States.
Department of Chemistry, University of California, Riverside, United States.
Biochem Biophys Res Commun. 2021 Mar 26;546:54-58. doi: 10.1016/j.bbrc.2021.01.088. Epub 2021 Feb 6.
Protein α-N-methylation is an evolutionarily conserved type of post-translational modification; however, little is known about the regulatory mechanisms for this modification. Methylation at the N position of adenosine in mRNAs is dynamic and modulates their stability, splicing, and translational efficiency. Here, we found that the expression of N-terminal methyltransferase 1 (NTMT1) protein is altered by depletion of those genes encoding the reader/writer/eraser proteins of N-methyladenosine (mA). We also observed that MRG15 is N-terminally methylated by NTMT1, and this methylation could also be modulated by reader/writer/eraser proteins of mA. Together, these results revealed a novel mA-based epitranscriptomic mechanism in regulating protein N-terminal methylation.
蛋白质α-N-甲基化是一种进化上保守的翻译后修饰类型;然而,对于这种修饰的调控机制知之甚少。mRNA 中腺苷 N 位的甲基化是动态的,调节其稳定性、剪接和翻译效率。在这里,我们发现 N-端甲基转移酶 1(NTMT1)蛋白的表达因编码 N-甲基腺苷(mA)的读取器/写入器/擦除器蛋白的基因缺失而改变。我们还观察到 MRG15 被 NTMT1 进行 N 端甲基化,并且这种甲基化也可以被 mA 的读取器/写入器/擦除器蛋白调节。综上所述,这些结果揭示了一种新的基于 mA 的转录后修饰机制,用于调节蛋白质 N 端甲基化。