The protein dimethyladenosine transferase 1 (Dim1) is a highly conserved protein occurring in organisms ranging from bacteria such as E. coli where it is named KsgA to humans. Since Dim1 is involved in the biogenesis of the small ribosomal subunit it is an essential protein. During ribosome biogenesis Dim1 acts as an rRNA modification enzyme and dimethylates two adjacent adenosine residues of the small ribosomal subunit rRNA. In eukaryotes it is also required to ensure the proper endonucleolytic processing of the small ribosomal subunit rRNA precursor. Recently, a third function was proposed for eukaryotic Dim1. Karbstein and coworkers suggested that Dim1 interacts with the essential ribosome assembly factor Fap7 and that Fap7 is responsible for the dissociation of Dim1 from the nascent small ribosomal subunit. Here, we report the backbone ¹H, ¹³C and ¹⁵N NMR resonance assignments for the 30.9 kDa Dim1 homologue from the hyperthermophilic archaeon Pyrococcus horikoshii (PhDim1) as a prerequisite for a detailed structural investigation of the PhDim1/PhFap7 interaction.

中文翻译：

---

1 H，13 C，15 N骨架NMR共振分配来自超嗜热古生火球菌的rRNA甲基转移酶Dim1。

蛋白质二甲基腺苷转移酶1（Dim1）是一种高度保守的蛋白质，存在于细菌等多种生物中，例如大肠杆菌它被人类称为KsgA。由于Dim1参与小核糖体亚基的生物发生，因此它是必需的蛋白质。在核糖体生物发生过程中，Dim1充当rRNA修饰酶，对小核糖体亚基rRNA的两个相邻的腺苷残基进行二甲基化。在真核生物中，还需要确保小核糖体亚基rRNA前体的正确核酸内切加工。最近，提出了针对真核Dim1的第三个功能。Karbstein和同事提出，Dim1与必需的核糖体装配因子Fap7相互作用，而Fap7负责使Dim1与新生的小核糖体亚基解离。在这里，我们报告主干¹ H，¹³ C和¹⁵来自超嗜热古生热球菌（Pyrococcus horikoshii）（Ph Dim1）的30.9 kDa Dim1同源物的N NMR共振分配是进行Ph Dim1 / Ph Fap7相互作用的详细结构研究的前提。