ISOLATION AND CHARACTERIZATION OF AN RNA LIGASE FROM HELA-CELLS
ISOLATION AND CHARACTERIZATION OF AN RNA LIGASE FROM HELA-CELLS
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DOI：
10.1073/pnas.82.3.684
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发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
HURWITZ, J
中科院分区：
文献类型：
--
作者：
PERKINS, KK;FURNEAUX, H;HURWITZ, J
从HeLa细胞中纯化了一种RNA连接酶，该酶在ATP或dATP存在下催化具有5“-羟基和2”，3“-环磷酸末端的线性RNA底物的分子内和分子间连接。在该反应中，2“，3”-环磷酸被掺入3“-5”-磷酸二酯键中，与Filipowicz等人的发现一致。纯化酶的活性取决于ATP或dATP、二价阳离子（Mg 2+）和5“-羟基，2”，3“-环磷酸封端的RNA底物的添加。与底物不发生连接。**图形 **。或.**图形 **。或用5 ″-磷酸、2 ″，3 ″-环磷酸封端的寡核糖核苷酸。
An RNA ligase was purified from HeLa cells, which catalyzes the intra- and intermolecular ligation of linear RNA substrates possessing 5''-hydroxyl and 2'',3''-cyclic phosphate termini in the presence of ATP or dATP. In this reaction, the 2'',3''-cyclic phosphate is incorporated into a 3''-5''-phosphodiester bond, in agreement with the findings of Filipowicz et al. The activity of the purified enzyme is dependent on the addition of ATP or dATP, a divalent cation (Mg2+), and 5''-hydroxyl, 2'', 3''-cyclic phosphate-terminated RNA substrates. No ligation occurs with the substrates .**GRAPHIC**. or .**GRAPHIC**. or with 5''-phosphate, 2'',3''-cyclic phosphate-terminated oligoribonucleotides.