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The amino-terminal domain of yeast U1-70K is necessary and sufficient for function.

机译:酵母U1-70K的氨基末端结构域对于功能是必需的和足够的。

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The Saccharomyces cerevisiae SNP1 gene encodes a protein that shares 30% amino acid identity with the mammalian U1 small nuclear ribonucleoprotein particle protein 70K (U1-70K). We have demonstrated that yeast strains in which the SNP1 gene was disrupted are viable but exhibit greatly increased doubling times and severe temperature sensitivity. Furthermore, snp1-null strains are defective in pre-mRNA splicing. We have tested deletion alleles of SNP1 for their ability to complement these phenotypes. We found that the highly conserved RNA recognition motif consensus domain of Snp1 is not required for complementation of the snp1-null growth or splicing defects nor for the in vivo association with the U1 small nuclear ribonucleoprotein particle. However, the amino-terminal domain of Snp1, less strongly conserved, is necessary and sufficient for complementation.
机译:酿酒酵母SNP1基因编码的一种蛋白质与哺乳动物U1小核糖核蛋白蛋白蛋白质70K(U1-70K)具有30%的氨基酸同一性。我们已经证明,其中SNP1基因被破坏的酵母菌株是可行的,但表现出倍增的时间大大增加,并且对温度的敏感性很高。此外,snp1-null菌株在mRNA前剪接中存在缺陷。我们已经测试了SNP1的缺失等位基因与这些表型互补的能力。我们发现Snp1的高度保守的RNA识别基序共有域不需要补充snp1-null的生长或剪接缺陷,也不需要与U1小核糖核蛋白颗粒的体内结合。但是,Snp1的氨基末端结构域的保守性较弱,对于互补而言是必要且足够的。

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