Bordonné R, Tarassov I
UPR 9005, Mécanismes Moléculaires de la Division Cellulaire et du Développement, IBMC, Strasbourg, France.
Gene. 1996 Oct 17;176(1-2):111-7. doi: 10.1016/0378-1119(96)00230-2.
Removal of introns from pre-messenger RNA (pre-mRNA) requires small nuclear RNAs (snRNAs) packaged into stable small ribonucleoprotein particles (snRNP). These snRNPs contain specific and common proteins also called Sm proteins. Correct assembly of the snRNAs with the common proteins is an essential step for the biogenesis of snRNP particles. We have identified a new Saccharomyces serevisiae gene, SME1 whose product shows 45% identity with the E core protein of human snRNP. The Sme1p contains the evolutionary conserved residues found in all Sm proteins. Combining genetic and biochemical experiments, we show that SME1 is an essential gene required for pre-mRNA splicing, cap modification and U1, U2, U4 and U5 snRNA stability. We show also that the human E core protein complements a yeast SME1 disruption demonstrating the functional equivalence of Sme1p and the human E core protein.
从前体信使核糖核酸（pre-mRNA）中去除内含子需要包装成稳定的小核糖核蛋白颗粒（snRNP）的小核核糖核酸（snRNA）。这些snRNP含有也被称为Sm蛋白的特异性和常见蛋白。snRNA与常见蛋白的正确组装是snRNP颗粒生物合成的关键步骤。我们鉴定出了一个新的酿酒酵母基因SME1，其产物与人snRNP的E核心蛋白有45%的同源性。Sme1p含有在所有Sm蛋白中都存在的进化保守残基。结合遗传学和生化实验，我们表明SME1是pre-mRNA剪接、帽修饰以及U1、U2、U4和U5 snRNA稳定性所必需的基因。我们还表明人E核心蛋白能够弥补酵母SME1的缺失，证明了Sme1p与人E核心蛋白的功能等效性。
