A tertiary interaction that links active-site domains to the 5′ splice site of a group II intron
A tertiary interaction that links active-site domains to the 5′ splice site of a group II intron
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DOI：
10.1038/35018589
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发表时间：
2000-07-20
期刊：
影响因子：
64.8
通讯作者：
Pyle, AM
中科院分区：
文献类型：
--
作者：
Boudvillain, M;de Lencastre, A;Pyle, AM
II组内含子是自剪接RNA，通常存在于植物、真菌、酵母和细菌的基因中（1，2）。第二组内含子是最大的天然核酶之一，其三级结构知之甚少。内含子的最保守区域是结构域5（D5），其与结构域1（D1）一起是由内含子催化的所有反应所需的（3）。尽管D5的重要性，它的空间关系和三级接触其他活性部位成分仍然模糊。此外，D5从未被直接置于内含子的催化位点。在这里，我们表明，一组三级相互作用（APDA-APDA '）连接D5和D1的催化必需区域，创建活性位点的框架并将其锚定在5'剪接位点。在真核剪接体中发现了与λ-λ相互作用的组分相似的高度保守的元件。
Group II introns are self-splicing RNAs that are commonly found in the genes of plants, fungi, yeast and bacteria(1,2). Little is known about the tertiary structure of group II introns, which are among the largest natural ribozymes. The most conserved region of the intron is domain 5 (D5), which, together with domain 1 (D1), is required for all reactions catalysed by the intron(3). Despite the importance of D5, its spatial relationship and tertiary contacts to other active-site constituents have remained obscure. Furthermore, D5 has never been placed directly at a site of catalysis by the intron. Here we show that a set of tertiary interactions (lambda-lambda') links catalytically essential regions of D5 and D1, creating the framework for an active-site and anchoring it at the 5' splice site. Highly conserved elements similar to components of the lambda-lambda' interaction are found in the eukaryotic spliceosome.