The Mrs1 splicing factor binds the bI3 group I intron at each of two tetraloop-receptor motifs.
The Mrs1 splicing factor binds the bI3 group I intron at each of two tetraloop-receptor motifs.
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DOI：
10.1371/journal.pone.0008983
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发表时间：
2010-02-01
期刊：
影响因子：
3.7
通讯作者：
Weeks KM
中科院分区：
文献类型：
--
作者：
Duncan CD;Weeks KM
大多数大型核酶需要蛋白质辅因子才能有效发挥功能。酵母线粒体bI 3 I组内含子需要两种蛋白质进行有效剪接，Mrs 1和bI 3成熟酶。Mrs 1已经从DNA连接分解酶进化为至少两个I组内含子的RNA辅因子;然而，RNA结合位点和Mrs 1促进剪接的机制尚不清楚。在这里，我们使用高通量的RNA结构分析表明，Mrs 1结合一个普遍存在的RNA三级结构基序，GNRA四环受体的相互作用，在两个网站的bI 3 RNA。Mrs 1也在类似的四环受体元件以及其他结构上相互作用，在自折叠Azoarcus I组内含子和RNase P酶中。因此，Mrs 1识别在四环受体基序中发现的一般特征。两个Mrs 1结合位点的鉴定现在使得有可能创建完整的六组分bI 3核糖核蛋白的模型。所有的蛋白质辅因子结合在RNA的外围，使得每一个长程RNA三级相互作用通过蛋白质结合而稳定，涉及Mrs 1或bI 3成熟酶。这项工作强调了强大的进化压力，以支持RNA三级结构与RNA结合的相互作用，如在核糖体，剪接体，和其他大型RNA机器。
Most large ribozymes require protein cofactors in order to function efficiently. The yeast mitochondrial bI3 group I intron requires two proteins for efficient splicing, Mrs1 and the bI3 maturase. Mrs1 has evolved from DNA junction resolvases to function as an RNA cofactor for at least two group I introns; however, the RNA binding site and the mechanism by which Mrs1 facilitates splicing were unknown. Here we use high-throughput RNA structure analysis to show that Mrs1 binds a ubiquitous RNA tertiary structure motif, the GNRA tetraloop-receptor interaction, at two sites in the bI3 RNA. Mrs1 also interacts at similar tetraloop-receptor elements, as well as other structures, in the self-folding Azoarcus group I intron and in the RNase P enzyme. Thus, Mrs1 recognizes general features found in the tetraloop-receptor motif. Identification of the two Mrs1 binding sites now makes it possible to create a model of the complete six-component bI3 ribonucleoprotein. All protein cofactors bind at the periphery of the RNA such that every long-range RNA tertiary interaction is stabilized by protein binding, involving either Mrs1 or the bI3 maturase. This work emphasizes the strong evolutionary pressure to bolster RNA tertiary structure with RNA-binding interactions as seen in the ribosome, spliceosome, and other large RNA machines.
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