tRNase Z：前路仍漫漫。
tRNase Z: the end is not in sight.
作者信息
Späth B, Canino G, Marchfelder A
机构信息
Molekulare Botanik, Universität Ulm, Albert-Einstein-Allee 11, 89069, Ulm, Germany.
出版信息
Cell Mol Life Sci. 2007 Sep;64(18):2404-12. doi: 10.1007/s00018-007-7160-5.
Although the enzyme tRNase Z has only recently been isolated, a plethora of data has already been acquired concerning the enzyme. tRNase Z is the endonuclease that catalyzes the removal of the tRNA 3' trailer, yielding the mature tRNA 3' end ready for CCA addition and aminoacylation. Another substrate cleaved by tRNase Z is the small chromogenic phosphodiester bis(p-nitrophenyl)phosphate (bpNPP), which is the smallest tRNase Z substrate known so far. Hitherto the biological function as tRNA 3'-end processing enzyme has been shown only in one prokaryotic and one eukaryotic organism, respectively. This review summarizes the present information concerning the two tRNase Z substrates pre-tRNA and bpNPP, as well as the metal requirements of tRNase Z enzymes.
尽管tRNase Z酶直到最近才被分离出来，但关于该酶已经获得了大量数据。tRNase Z是一种核酸内切酶，它催化去除tRNA的3'拖尾序列，产生成熟的tRNA 3'末端，为添加CCA和氨酰化做好准备。tRNase Z切割的另一种底物是小分子显色磷酸二酯双（对硝基苯基）磷酸酯（bpNPP），它是迄今为止已知的最小的tRNase Z底物。迄今为止，作为tRNA 3'末端加工酶的生物学功能仅分别在一种原核生物和一种真核生物中得到证实。这篇综述总结了目前有关tRNase Z的两种底物——前体tRNA和bpNPP以及tRNase Z酶的金属需求的信息。
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