The catalytic core of RNase P

The catalytic core of RNase P
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DOI:
10.1093/nar/24.8.1497
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发表时间:
1996-04-15
影响因子:
14.9
通讯作者:
Vold, BS
Vold, BS
中科院分区:
生物学2区
文献类型:
--
作者:
Green, CJ;RiveraLeon, R;Vold, BS

文献摘要

被引文献

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大肠杆菌 RNase P 催化 RNA 成分缺失残基 87-241 的缺失突变体保留了与蛋白质成分相互作用形成功能性催化剂的能力。这个系统发育保守区域的删除显着增加了K-m,表明删除的结构可能对于与前体tRNA底物的结合很重要,但对于切割反应并不重要。在某些反应条件下,这个RNase P删除突变体可以成为相对非特异性的核酸酶,表明这个RNA的催化中心可能更加暴露。 RNase P 的催化核心由 RNase P RNA 的 377 个残基中不到三分之一组成。
A deletion mutant of the catalytic RNA component of Escherichia coli RNase P missing residues 87-241 retains the ability to interact with the protein component to form a functional catalyst. The deletion of this phylogenetically conserved region significantly increases the K-m, indicating that the deleted structures may be important for binding to the precursor tRNA substrate but not for the cleavage reaction, Under some reaction conditions, this RNase P deletion mutant can become a relatively non-specific nuclease, indicating that this RNA's catalytic center may be more exposed. The catalytic core of the RNase P is formed by less than one third of the 377 residues of the RNase P RNA.