Multiple terminal uridylyltransferases of trypanosomes
Multiple terminal uridylyltransferases of trypanosomes
复制标题
DOI：
10.1016/j.febslet.2004.07.004
复制
发表时间：
2004-08-13
期刊：
影响因子：
3.5
通讯作者：
Simpson, L
中科院分区：
文献类型：
--
作者：
Aphasizhev, R;Aphasizheva, I;Simpson, L
已经报道了在几种单细胞和后生动物的生物体中据报道将尿液残基的转移酶活性。到目前为止，参与锥虫线粒体中尿苷插入/缺失mRNA涉及的两个末端尿液转移酶（诱导酶）是唯一已知的UTP特异性酶。在这里，我们证明了编辑培养酶的蛋白质序列可用于通过数据挖掘来预测新型UTP特异性酶。表达了来自锥虫锥虫的得分最高的开放式阅读框，并纯化了重组蛋白。这种酶催化了一种过程中的UMP掺入，并且不定位于线粒体，提示非编辑生物学功能。 （c）2004年由Elsevier B.V.代表欧洲生物化学社会联合会出版。
The transferase activities that add uridylyl residues to RNA have been reported in several unicellular and metazoan organisms. Thus far, the two terminal uridylyltransferases (TUTases) involved in uridine insertion/deletion mRNA editing in mitochondria of trypanosomes were the only known enzymes with confirmed UTP specificity. Here, we demonstrate that protein sequences of editing TUTases may be used to predict novel UTP-specific enzymes by data mining. The highest-scoring open reading frame from Trypanosoma brucei was expressed and recombinant protein purified. This enzyme catalyzes a processive UMP incorporation and is not localized to the mitochondria suggesting a non-editing biological function. (C)2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.