Kataoka N, Yong J, Kim V N, Velazquez F, Perkinson R A, Wang F, Dreyfuss G
Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.
Mol Cell. 2000 Sep;6(3):673-82. doi: 10.1016/s1097-2765(00)00065-4.
We describe a novel RNA binding protein, Y14, a predominantly nuclear nucleocytoplasmic shuttling protein. Interestingly, Y14 associates preferentially with mRNAs produced by splicing but not with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Y14 associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. Splicing of a single intron is sufficient for Y14 association. Y14-containing nuclear complexes are different from general hnRNP complexes. They contain hnRNP proteins and several unique proteins including the mRNA export factor TAP. Thus, Y14 defines novel intermediates in the pathway of gene expression, postsplicing nuclear preexport mRNPs, and newly exported cytoplasmic mRNPs, whose composition is established by splicing. These findings suggest that pre-mRNA splicing imprints mRNA with a unique set of proteins that persists in the cytoplasm and thereby communicates the history of the transcript.
我们描述了一种新型RNA结合蛋白Y14,它是一种主要在细胞核中穿梭于核质之间的蛋白。有趣的是,Y14优先与通过剪接产生的mRNA结合,而不与前体mRNA、内含子或由无内含子cDNA产生的mRNA结合。Y14与核mRNA和新输出到细胞质的mRNA都有关联。单个内含子的剪接足以使Y14与之结合。含有Y14的核复合物不同于一般的hnRNP复合物。它们包含hnRNP蛋白和几种独特的蛋白,包括mRNA输出因子TAP。因此,Y14定义了基因表达途径中的新型中间体,即剪接后核输出前的mRNA颗粒以及新输出到细胞质的mRNA颗粒,其组成由剪接确定。这些发现表明,前体mRNA剪接为mRNA印记了一组独特的蛋白质,这些蛋白质在细胞质中持续存在,从而传递了转录本的历史。