A structural and functional study of plastid RNAs homologous to catalytic bacterial RNase P RNA
A structural and functional study of plastid RNAs homologous to catalytic bacterial RNase P RNA
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DOI：
10.1016/s0378-1119(03)00831-x
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发表时间：
2003-12-04
期刊：
影响因子：
3.5
通讯作者：
Vioque, A
中科院分区：
文献类型：
--
作者：
de la Cruz, J;Vioque, A
核糖核酸酶P（Ribonuclease P，RNase P）是一种核糖核蛋白，含有一个必需的RNA亚基，是转运RNA 5'端成熟所必需的酶。这种RNA（P RNA）是细菌和某些细菌中RNase P的催化组分。在蓝藻、紫紫菜和肾形藻的叶绿体基因组中编码一种假定的P RNA。在任何情况下，在细菌和一些古细菌的P RNA是功能性的条件下，质体的P RNA在体外是有活性的。通过使用铅离子诱导的水解，我们得出结论，催化缺陷是最有可能由于扰动的质体P RNA的全球结构相比，细菌的对应物。因此，质体P RNA不能与前体tRNA底物结合。我们讨论这些结果的背景下，质体和RNase P的进化。(C)2003 Elsevier B.V.保留所有权利。
Ribonuclease P (RNase P), the ubiquitous enzyme required for 5' maturation of transfer RNA, is a ribonucleoprotein containing an essential RNA subunit. This RNA (P RNA) is the catalytic component of RNase P in Bacteria and some Archaea. A putative P RNA is encoded in the chloroplast genome of three algae: Cyanophora paradoxa, Porphyra purpurea and Nephroselmis olivacea. In no case, the P RNAs from the plastids were active in vitro in conditions where bacterial and some archaeal P RNAs are functional. By using lead-ion-induced hydrolysis, we conclude that the catalytic deficiency is most likely due to the perturbation of the global structure of the plastid P RNAs compared to the bacterial counterpart. As a consequence, the plastid P RNAs are unable to bind to the precursor tRNA substrates. We discuss these results in the context of plastid and RNase P evolution. (C) 2003 Elsevier B.V. All rights reserved.