Gerber A P, Keller W
Department of Cell Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland.
Science. 1999 Nov 5;286(5442):1146-9. doi: 10.1126/science.286.5442.1146.
Several transfer RNAs (tRNAs) contain inosine (I) at the first position of their anticodon (position 34); this modification is thought to enlarge the codon recognition capacity during protein synthesis. The tRNA-specific adenosine deaminase of Saccharomyces cerevisiae that forms I(34) in tRNAs is described. The heterodimeric enzyme consists of two sequence-related subunits (Tad2p/ADAT2 and Tad3p/ADAT3), both of which contain cytidine deaminase (CDA) motifs. Each subunit is encoded by an essential gene (TAD2 and TAD3), indicating that I(34) is an indispensable base modification in elongating tRNAs. These results provide an evolutionary link between the CDA superfamily and RNA-dependent adenosine deaminases (ADARs/ADATs).
几种转运RNA(tRNA)在其反密码子的第一位(第34位)含有次黄嘌呤(I);这种修饰被认为在蛋白质合成过程中扩大了密码子识别能力。本文描述了酿酒酵母中在tRNA中形成I(34)的tRNA特异性腺苷脱氨酶。这种异二聚体酶由两个序列相关的亚基(Tad2p/ADAT2和Tad3p/ADAT3)组成,这两个亚基都含有胞苷脱氨酶(CDA)基序。每个亚基由一个必需基因(TAD2和TAD3)编码,这表明I(34)是延伸tRNA中不可或缺的碱基修饰。这些结果提供了CDA超家族与RNA依赖性腺苷脱氨酶(ADARs/ADATs)之间的进化联系。