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特定的 Y14 结构域介导其核质穿梭和与剪接 mRNA 的结合。

Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA.

机构信息

Medical Top Track Program, Medical Research Institute, Tokyo Dental and Medical University, Tokyo 113-8510, Japan.

出版信息

Sci Rep. 2011;1:92. doi: 10.1038/srep00092. Epub 2011 Sep 14.

Abstract

Pre-mRNA splicing deposits multi-protein complexes, termed exon junction complexes (EJCs), on mRNAs near exon-exon junctions. The core of EJC consists of four proteins, eIF4AIII, MLN51, Y14 and Magoh. Y14 is a nuclear protein that can shuttle between the nucleus and the cytoplasm, and binds specifically to Magoh. Here we delineate a Y14 nuclear localization signal that also confers its nuclear export, which we name YNS. We further identified a 12-amino-acid peptide near Y14's carboxyl terminus that is required for its association with spliced mRNAs, as well as for Magoh binding. Furthermore, the Y14 mutants, which are deficient in binding to Magoh, could still be localized to the nucleus, suggesting the existence of both the nuclear import pathway and function for Y14 unaccompanied by Magoh.

摘要

前体 mRNA 剪接在 mRNA 上临近外显子-内含子交界处沉积多蛋白复合物,称为外显子结合复合物(EJCs)。EJC 的核心由四种蛋白组成,分别是 eIF4AIII、MLN51、Y14 和 Magoh。Y14 是一种核蛋白,可在核和细胞质之间穿梭,并特异性地与 Magoh 结合。在这里,我们描述了一个 Y14 核定位信号,它也赋予了 Y14 的核输出,我们将其命名为 YNS。我们进一步鉴定了 Y14 羧基末端附近的一个 12 个氨基酸肽段,该肽段对于 Y14 与剪接 mRNA 的结合以及与 Magoh 的结合都是必需的。此外,与 Magoh 结合缺陷的 Y14 突变体仍能定位于细胞核,这表明存在 Y14 与 Magoh 不结合的核输入途径和功能。

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