SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
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DOI：
10.1016/s1097-2765(03)00089-3
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发表时间：
2003-03-01
期刊：
影响因子：
16
通讯作者：
Steitz, JA
中科院分区：
文献类型：
--
作者：
Huang, YQ;Gattoni, R;Steitz, JA
已知与TAP/NXF 1（用于一般mRNA输出的主要受体）配对的唯一哺乳动物RNA结合衔接子蛋白是REF家族的成员。我们证明，至少有三个穿梭SR（丝氨酸/丝氨酸丰富）蛋白质相互作用的TAP/NXF 1结合参考文献的相同结构域。包括9 G8和SRp 20，先前显示促进无内含子RNA的输出。来自9 G8的N末端的肽在体外抑制REF和SR蛋白与TAP/NXF 1的结合，这一发现为竞争性相互作用提供了论据。在非洲爪蟾卵母细胞中，9 G8的N末端对mRNA从细胞核的输出表现出显性负效应，而加入过量的TAP/NXF 1克服了这种抑制。因此，包括SR蛋白在内的多个衔接子最有可能协作以募集TAP/NXF 1的多个拷贝用于有效的mRNA输出。
The only mammalian RNA binding adapter proteins known to partner with TAP/NXF1, the primary receptor for general mRNA export, are members of the REF family. We demonstrate that at least three shuttling SR (serine/arginine-rich) proteins interact with the same domain of TAP/NXF1 that binds REFs. Included are 9G8 and SRp20, previously shown to promote the export of intronless RNAs. A peptide derived from the N terminus of 9G8 inhibits the binding of both REF and SR proteins to TAP/NXF1 in vitro, and this finding argues for competitive interactions. In Xenopus oocytes, the N terminus of 9G8 exhibits a dominant-negative effect on mRNA export from the nucleus, while addition of excess TAP/NXF1 overcomes this inhibition. Thus, multiple adapters including SR proteins most likely cooperate to recruit multiple copies of TAP/NXF1 for efficient mRNA export.