Swanson M S, Dreyfuss G
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208.
Mol Cell Biol. 1988 May;8(5):2237-41. doi: 10.1128/mcb.8.5.2237-2241.1988.
Several proteins of heterogeneous nuclear ribonucleoprotein (hnRNP) particles display very high binding affinities for different ribonucleotide homopolymers. The specificity of some of these proteins at high salt concentrations and in the presence of heparin allows for their rapid one-step purification from HeLa nucleoplasm. We show that the hnRNP C proteins are poly(U)-binding proteins and compare their specificity to that of the previously described cytoplasmic poly(A)-binding protein. These findings provide a useful tool for the classification and purification of hnRNP proteins from various tissues and organisms and indicate that different hnRNP proteins have different RNA-binding specificities.
几种不均一核核糖核蛋白(hnRNP)颗粒的蛋白质对不同的核糖核苷酸同聚物表现出非常高的结合亲和力。其中一些蛋白质在高盐浓度和肝素存在下的特异性使得它们能够从HeLa细胞核质中快速一步纯化。我们表明hnRNP C蛋白是聚(U)结合蛋白,并将它们的特异性与先前描述的细胞质聚(A)结合蛋白的特异性进行比较。这些发现为从各种组织和生物体中分类和纯化hnRNP蛋白提供了有用的工具,并表明不同的hnRNP蛋白具有不同的RNA结合特异性。