Dauwalder B, Mattox W
Department of Molecular Genetics, University of Texas, MD Anderson Cancer Center, 1515 Holcombe Blvd, Box 45, Houston, TX 77030, USA.
EMBO J. 1998 Oct 15;17(20):6049-60. doi: 10.1093/emboj/17.20.6049.
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 dU2AF50 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.
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)。这些结构域被认为有助于蛋白质-蛋白质相互作用,而这种相互作用在可变剪接的调控中至关重要。通过结构域交换策略,我们测试了几种蛋白质的RS结构域在体内替代果蝇剪接调节因子TRA-2中必需RS结构域的能力。通过多个标准发现,RS结构域在支持TRA-2剪接调节功能的能力上有显著差异。dU2AF50的RS结构域功能高效,而dSRp55蛋白的RS结构域则不然。此外,我们发现在将融合蛋白引导至TRA-2与精母细胞染色体结合的离散核内亚位点的能力方面,RS结构域也存在类似差异。这些结果表明,RS结构域在体内并非都具有同等功能。