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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Catalytically critical nucleotide in domain 5 of a group II intron.
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Catalytically critical nucleotide in domain 5 of a group II intron.

机译:II组内含子的结构域5中的催化关键核苷酸。

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摘要

Domain 5 (D5) is a small hairpin structure within group II introns. A bimolecular assay system depends on binding by D5 to an intron substrate for self-splicing activity. In this study, mutations in D5 identify two among six nearly invariant nucleotides as being critical for 5' splice junction hydrolysis but unimportant for binding. A mutation at another site in D5 blocks binding. Thus, mutations can distinguish two D5 functions: substrate binding and catalysis. The secondary structure of D5 may resemble helix I formed by the U2 and U6 small nuclear RNAs in the eukaryotic spliceosome. Our results support a revision of the previously proposed correspondence between D5 and helix I on the basis of the critical trinucleotide 5'-AGC-3' present in both. We suggest that this trinucleotide plays a similar role in promoting the chemical reactions for both splicing systems.
机译:域5(D5)是II组内含子中的一个小发夹结构。双分子测定系统依靠D5与内含子底物的结合来实现自我剪接活性。在这项研究中,D5中的突变确定了6个几乎不变的核苷酸中的2个对5'剪接连接水解至关重要,但对结合而言并不重要。 D5中另一个位点的突变会阻止结合。因此,突变可以区分两个D5功能:底物结合和催化。 D5的二级结构可能类似于由真核剪接体中的U2和U6小核RNA形成的螺旋I。我们的结果支持基于之前提出的D5和螺旋I之间存在的关键三核苷酸5'-AGC-3'的对应关系的修订。我们建议这种三核苷酸在促进两个剪接系统的化学反应中起相似的作用。

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