Rymond B C, Rokeach L A, Hoch S O
T.H. Morgan School of Biological Sciences, University of Kentucky, Lexington 40506-0225.
Nucleic Acids Res. 1993 Jul 25;21(15):3501-5. doi: 10.1093/nar/21.15.3501.
Parallel investigations of yeast and metazoan pre-mRNA splicing have documented enormous complexity in the nucleic acid and protein components of the cellular splicing apparatus, the spliceosome. The degree to which yeast and metazoan spliceosomal proteins differ in composition and structure is currently unknown. In this report we demonstrate that the human small nuclear ribonucleoprotein (snRNP) polypeptide D1 complements the cell lethality, splicing deficiency, and snRNA instability phenotypes associated with a yeast smd1 null allele. Mutational analysis of yeast SMD1, guided by a comparison of the predicted yeast and human proteins, reveals that a large, nonconserved portion of Smd1p is dispensable for biological activity. These observations firmly establish D1 as an essential component of the cellular splicing apparatus and suggest that yeast and metazoa are remarkably similar in the polypeptides guiding early snRNP assembly.
对酵母和后生动物前体mRNA剪接的平行研究表明，细胞剪接装置即剪接体的核酸和蛋白质成分极其复杂。目前尚不清楚酵母和后生动物剪接体蛋白在组成和结构上的差异程度。在本报告中，我们证明人类小核核糖核蛋白（snRNP）多肽D1可弥补与酵母smd1无效等位基因相关的细胞致死性、剪接缺陷和snRNA不稳定性表型。通过比较预测的酵母和人类蛋白质对酵母SMD1进行突变分析，结果显示Smd1p中一大段非保守部分对于生物活性是可有可无的。这些观察结果确凿地证实D1是细胞剪接装置的重要组成部分，并表明酵母和后生动物在引导早期snRNP组装的多肽方面非常相似。
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