古菌中 tRNA 的硒代修饰需要一个双组分硫氰酸酶。
Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme.
机构信息
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
出版信息
FEBS Lett. 2012 Mar 23;586(6):717-21. doi: 10.1016/j.febslet.2012.01.024. Epub 2012 Jan 27.
Abstract
5-Methylaminomethyl-2-selenouridine (mnm(5)Se(2)U) is found in the first position of the anticodon in certain tRNAs from bacteria, archaea and eukaryotes. This selenonucleoside is formed in Escherichia coli from the corresponding thionucleoside mnm(5)S(2)U by the monomeric enzyme YbbB. This nucleoside is present in the tRNA of Methanococcales, yet the corresponding 2-selenouridine synthase is unknown in archaea and eukaryotes. Here we report that a bipartite ybbB ortholog is present in all members of the Methanococcales. Gene deletions in Methanococcus maripaludis and in vitro activity assays confirm that the two proteins act in trans to form in tRNA a selenonucleoside, presumably mnm(5)Se(2)U. Phylogenetic data suggest a primal origin of seleno-modified tRNAs.
摘要
5-甲基氨基甲基-2-硒代尿苷（mnm(5)Se(2)U）存在于某些细菌、古菌和真核生物 tRNA 的反密码子的第一位。这种硒核苷是由大肠杆菌中的单体酶 YbbB 从相应的硫代核苷 mnm(5)S(2)U 形成的。这种核苷存在于 Methanococcales 的 tRNA 中，但在古菌和真核生物中，相应的 2-硒代尿苷合酶是未知的。在这里，我们报告说，二聚体 ybbB 直系同源物存在于 Methanococcales 的所有成员中。Methanococcus maripaludis 的基因缺失和体外活性测定证实，这两种蛋白以反式作用于 tRNA 形成硒核苷，可能是 mnm(5)Se(2)U。系统发育数据表明，硒修饰的 tRNA 具有原始起源。
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