Analysis of the functional specificity of RS domains in vivo
Analysis of the functional specificity of RS domains in vivo
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DOI：
10.1093/emboj/17.20.6049
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发表时间：
1998-10-15
期刊：
影响因子：
11.4
通讯作者：
Mattox, W
中科院分区：
文献类型：
--
作者：
Dauwalder, B;Mattox, W
许多剪接因子含有富含精氨酸和丝氨酸的广泛区域（RS结构域）。这些结构域被认为促进蛋白质-蛋白质相互作用，这在可变剪接的调节中至关重要。使用结构域交换策略，我们已经测试了从几个蛋白质的RS域的能力，在体内的果蝇剪接调节TRA-2中的一个重要的RS域的替代。通过几个标准，发现RS结构域在其支持TRA-2的剪接调节功能的能力上显著不同。dU 2AF（50）的RS结构域有效地起作用，而dSRp 55蛋白的RS结构域不起作用。此外，我们发现类似的差异RS域的能力，直接融合蛋白到离散的亚核位点TRA-2协会与精母细胞染色体。这些结果表明，RS结构域在体内并不都是功能等同的。
A number of splicing factors contain extensive regions that are rich in arginine and serine (RS domains). These domains are thought to facilitate protein-protein interactions that are critical in the regulation of alternative splicing. Using a domain swap strategy, we have tested the ability of RS domains from several proteins to substitute in vivo for an essential RS domain in the Drosophila splicing regulator TRA-2. By several criteria, RS domains were found to vary significantly in their ability to support the splicing regulation functions of TRA-2. The RS domain of dU2AF(50) functioned efficiently; while that of the dSRp55 protein did not. Moreover, we find similar differences in the ability of RS domains to direct fusion proteins to discrete subnuclear sites at which TRA-2 associates with spermatocyte chromosomes. These results indicate that RS domains are not all functionally equivalent in vivo.