Okada N, Noguchi S, Kasai H, Shindo-Okada N, Ohgi T, Goto T, Nishimura S
J Biol Chem. 1979 Apr 25;254(8):3067-73.
The guanine insertion enzyme isolated from Escherichia coli (tRNA transglycosylase) catalyzed the incorporation of bases of Q (queuosine) precursors into E. coli undermodified tRNAAsn and tRNATyr. These bases of Q precursors were inserted in the first position of the anticodon of tRNASn and tRNATyr, replacing guanine originally located in that position. This is a novel type of post-transcriptional modification, inserting a modified base into the polynucleotide chain by cleavage of the N--C glycoside bond without breakage of the phosphodiester bond. One of the bases of Q precursors, 7-(aminomethyl)-7-deazaguanine, was found in the acid-soluble fraction of E. coli cells, supporting the conclusion that formation of Q, 7-(3,4-trans-4,5-cis-dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanosine, in tRNA in vivo actually proceeds by the tRNA transglycosylase reaction.
从大肠杆菌中分离出的鸟嘌呤插入酶(tRNA转糖基酶)催化将Q(queuosine)前体的碱基掺入大肠杆菌中修饰不足的tRNAAsn和tRNATyr。这些Q前体的碱基插入到tRNASn和tRNATyr反密码子的第一位,取代原本位于该位置的鸟嘌呤。这是一种新型的转录后修饰,通过N--C糖苷键的断裂将修饰碱基插入多核苷酸链,而不破坏磷酸二酯键。在大肠杆菌细胞的酸溶性部分中发现了Q前体的一种碱基,7-(氨甲基)-7-脱氮鸟嘌呤,这支持了tRNA转糖基酶反应实际上在体内tRNA中形成Q,即7-(3,4-反式-4,5-顺式-二羟基-1-环戊烯-3-基氨甲基)-7-脱氮鸟苷的结论。