Gallinaro H, Puvion E, Kister L, Jacob M
EMBO J. 1983;2(6):953-60. doi: 10.1002/j.1460-2075.1983.tb01527.x.
Nuclear matrix and heterogeneous nuclear ribonucleoprotein (hnRNP) were compared to establish whether premessenger RNA (premRNA) was associated with a same constituent in both structures. The isolation of nuclear matrix included the removal of chromatin and of 0.4 M KCl-soluble material. HnRNP, isolated by a standard method was also treated by 0.4 M KCl. Both isolation procedures caused the removal of DNA, histones, a fraction of small nuclear RNA and of nonhistone proteins including the hnRNP proteins in the 30 000-40 000 mol. wt. range. High resolution autoradiography showed that hnRNA remained associated with the residual fibrils in both structures. They both contained the same premRNA and maturation products as shown by the analysis of the transcripts of the early region 3 of adenovirus 2. In addition, the small nuclear RNA and protein of the salt-resistant complexes were also present in the matrix. The results are compatible with the idea that the salt-resistant complexes from hnRNP constitute the fibrils associated with premRNA in the nucleoplasmic matrix. The fibrils may be the basic unit of splicing and their organization in matrix might provide the spatial configuration necessary for regulation.
对核基质和不均一核核糖核蛋白（hnRNP）进行比较，以确定前体信使RNA（premRNA）是否与这两种结构中的相同成分相关联。核基质的分离包括去除染色质和0.4M KCl可溶性物质。通过标准方法分离的hnRNP也用0.4M KCl处理。两种分离程序都导致DNA、组蛋白、一部分小核RNA以及包括30000-40000分子量范围内的hnRNP蛋白在内的非组蛋白的去除。高分辨率放射自显影显示，hnRNA在两种结构中均与残留纤维相关联。如对腺病毒2早期区域3转录本的分析所示，它们都含有相同的premRNA和成熟产物。此外，耐盐复合物的小核RNA和蛋白质也存在于基质中。这些结果与以下观点一致，即hnRNP的耐盐复合物构成了核质基质中与premRNA相关联的纤维。这些纤维可能是剪接的基本单位，它们在基质中的组织可能提供调节所需的空间构型。
