嗜热栖热菌HB27中tRNA（腺苷-1-）-甲基转移酶的纯化与特性分析
Purification and characterization of tRNA(adenosine-1-)-methyltransferase from Thermus thermophilus HB27.
作者信息
Yamazaki N, Hori H, Ozawa K, Nakanishi S, Ueda T, Kumagai I, Watanabe K, Nishikawa K
机构信息
Department of Biological Sciences, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
出版信息
Nucleic Acids Symp Ser. 1992(27):141-2.
A58, the conserved adenosine residue in the T psi C loop of tRNAs, is methylated to m1A 58 in an extreme thermophile, Thermus thermophilus HB27. The enzyme catalyzing this methyltransfer reaction was purified from the thermophle. The substrate specificity of the enzyme was investigated by using tRNA fragments. The enzyme can transfer the methyl group to the 3'-half fragment of E. coli initiator tRNA, indicating that the main recognition site of the enzyme exists in the 3' half of tRNA including the T-loop and the T-stem.
在嗜热栖热菌HB27（一种极端嗜热菌）中，tRNA反密码子环上保守的腺苷残基A58被甲基化为1-甲基腺苷（m1A 58）。催化这种甲基转移反应的酶是从嗜热菌中纯化得到的。通过使用tRNA片段研究了该酶的底物特异性。该酶能够将甲基转移到大肠杆菌起始tRNA的3'-半片段上，这表明该酶的主要识别位点存在于tRNA的3'半部分，包括T环和T茎。
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