Gerber A, Grosjean H, Melcher T, Keller W
Department of Cell Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.
EMBO J. 1998 Aug 17;17(16):4780-9. doi: 10.1093/emboj/17.16.4780.
We have identified an RNA-specific adenosine deaminase (termed Tad1p/scADAT1) from Saccharomyces cerevisiae that selectively converts adenosine at position 37 of eukaryotic tRNAAla to inosine. The activity of purified recombinant Tad1p depends on the conformation of its tRNA substrate and the enzyme was found to be inactive on all other types of RNA tested. Mutant strains in which the TAD1 gene is disrupted are viable but lack Tad1p enzyme activity and their tRNAAla is not modified at position A37. Transformation of the mutant cells with the TAD1 gene restored enzyme activity. Tad1p has significant sequence similarity with the mammalian editing enzymes which act on specific precursor-mRNAs and on long double-stranded RNA. These findings suggest an evolutionary link between pre-mRNA editing and tRNA modification.
我们从酿酒酵母中鉴定出一种RNA特异性腺苷脱氨酶(称为Tad1p/scADAT1),它能选择性地将真核生物丙氨酸转运RNA(tRNAAla)第37位的腺苷转化为肌苷。纯化的重组Tad1p的活性取决于其tRNA底物的构象,并且发现该酶对所有其他测试类型的RNA均无活性。TAD1基因被破坏的突变菌株是可存活的,但缺乏Tad1p酶活性,并且它们的tRNAAla在A37位未被修饰。用TAD1基因转化突变细胞可恢复酶活性。Tad1p与作用于特定前体信使RNA和长双链RNA的哺乳动物编辑酶具有显著的序列相似性。这些发现表明前体信使RNA编辑与tRNA修饰之间存在进化联系。