一种220千道尔顿的哺乳动物蛋白在剪接体中与前体信使核糖核酸结合：酵母PRP8蛋白的潜在同源物。
A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome: a potential homologue of the yeast PRP8 protein.
作者信息
Garcia-Blanco M A, Anderson G J, Beggs J, Sharp P A
机构信息
Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.
出版信息
Proc Natl Acad Sci U S A. 1990 Apr;87(8):3082-6. doi: 10.1073/pnas.87.8.3082.
A mammalian protein of approximately 220 kDa (p220) was UV-crosslinked to precursor mRNAs (pre-mRNAs) under splicing conditions. The kinetics and biochemical requirements of the UV-crosslinking of p220 corresponded to the kinetics and biochemical requirements of spliceosome formation. On Western blots, antibodies against the yeast splicing factor PRP8 recognized a doublet of proteins, the faster migrating of which comigrated with p220. Furthermore, UV-crosslinked p220 was immunoprecipitated with anti-PRP8 antisera. These results suggest structural conservation of the splicing factor PRP8 from yeast to mammals and show that this protein is in close proximity to the pre-mRNA in the spliceosome.
在剪接条件下，一种约220 kDa的哺乳动物蛋白（p220）与前体mRNA（pre-mRNA）发生了紫外线交联。p220紫外线交联的动力学和生化要求与剪接体形成的动力学和生化要求一致。在蛋白质免疫印迹分析中，针对酵母剪接因子PRP8的抗体识别出一组双重蛋白，其中迁移速度较快的蛋白与p220共迁移。此外，紫外线交联的p220用抗PRP8抗血清进行了免疫沉淀。这些结果表明，从酵母到哺乳动物，剪接因子PRP8在结构上具有保守性，并表明该蛋白在剪接体中与前体mRNA紧密相邻。
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