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精氨酸和丝氨酸富集蛋白(Arginine/ser ine-rich proteins,SR proteins)是剪切复合体中的重要成员.SR蛋白能够通过C端结构域相互作用并参与前体信使RNA的组成性剪切及可变剪切加工过程.为了揭示水稻SR蛋白间的相互作用网络,利用GAL4酵母双杂交系统,对来自不同亚家族的6个水稻SR蛋白进行相互作用分析.结果发现,来自两个不同亚家族的SR基因SCL30a和SC34共转化酵母能在相应缺陷培养基上生长,α-半乳糖苷酶活性约为对照的17倍,表明两者存在直接的相互作用关系,同时也暗示水稻可能通过SR蛋白直接相互作用,对重要基因的剪切加工及表达进行再次精细调控以应对外界复杂的环境变化.
Arginine / serine-rich proteins (SR proteins) are important members of the shearing complex.SR proteins interact through the C-terminal domain and participate in the constitutive scission of the precursor messenger RNA Cutting and variable shear processing.In order to reveal the network of SR protein interactions in rice, six rice SR proteins from different subfamilies were analyzed for interaction using the GAL4 yeast two-hybrid system and found that the SR proteins from two different The subfamily SR gene SCL30a and SC34 co-transformed yeast could grow on the corresponding deficient medium, and the α-galactosidase activity was about 17 times that of the control, indicating that there was a direct interaction between the two genes and suggesting that rice might pass SR protein direct interaction, the important gene of shear processing and expression again finely adjusted to deal with complex changes in the environment.