酵母U1-70K的氨基末端结构域对于其功能而言是必需且充分的。
The amino-terminal domain of yeast U1-70K is necessary and sufficient for function.
作者信息
Hilleren P J, Kao H Y, Siliciano P G
机构信息
Department of Biochemistry, University of Minnesota, Minneapolis 55455, USA.
出版信息
Mol Cell Biol. 1995 Nov;15(11):6341-50. doi: 10.1128/MCB.15.11.6341.
Abstract
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.
摘要
酿酒酵母SNP1基因编码一种蛋白质，该蛋白质与哺乳动物U1小核核糖核蛋白颗粒蛋白70K（U1 - 70K）具有30%的氨基酸同一性。我们已经证明，SNP1基因被破坏的酵母菌株是可行的，但表现出显著增加的倍增时间和严重的温度敏感性。此外，snp1缺失菌株在mRNA前体剪接方面存在缺陷。我们已经测试了SNP1的缺失等位基因互补这些表型的能力。我们发现，Snp1高度保守的RNA识别基序共有结构域对于snp1缺失的生长或剪接缺陷的互补以及与U1小核核糖核蛋白颗粒的体内结合并非必需。然而，Snp1的氨基末端结构域保守性较弱，对于互补是必要且充分的。
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