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Crystal structures of a group II intron maturase reveal a missing link in spliceosome evolution

机译:II组内含子成熟酶的晶体结构揭示了剪接体进化过程中的缺失环节。

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摘要

Group II introns are self-splicing ribozymes that are essential in many organisms, and they have been hypothesized to share a common evolutionary ancestor with the spliceosome. Although structural similarity of RNA components supports this connection, it is of interest to determine whether associated protein factors also share an evolutionary heritage. Here we present the crystal structures of reverse transcriptase (RT) domains from two group II intron-encoded proteins (maturases) from Roseburia intestinalis and Eubacterium rectale, obtained at 1.2-angstrom and 2.1-angstrom resolution, respectively. These domains are more similar in architecture to the spliceosomal Prp8 RT-like domain than to any other RTs, and they share substantial similarity with flaviviral RNA polymerases. The RT domain itself is sufficient for binding intron RNA with high affinity and specificity, and it is contained within an active RT enzyme. These studies provide a foundation for understanding structure-function relationships within group II intron-maturase complexes.
机译:第二组内含子是在许多生物中必不可少的自剪接核酶,据推测它们与剪接体具有共同的进化祖先。尽管RNA成分的结构相似性支持这种联系,但确定相关的蛋白质因子是否也具有进化遗传是有意义的。在这里,我们介绍了分别从1.2埃和2.1埃的分辨率获得的来自Roseburia intestinalis和Eubacter rectale的两个第二组内含子编码蛋白(成熟酶)的逆转录酶(RT)域的晶体结构。这些结构域在结构上与剪接的Prp8 RT样结构域比其他任何RT相似,并且它们与黄病毒RNA聚合酶具有基本相似性。 RT结构域本身足以以高亲和力和特异性结合内含子RNA,并且包含在活性RT酶中。这些研究为理解第二组内含子-成熟酶复合物中的结构-功能关系提供了基础。

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