Mattern K A, Humbel B M, Muijsers A O, de Jong L, van Driel R
E.C. Slater Instituut, University of Amsterdam, The Netherlands.
J Cell Biochem. 1996 Aug;62(2):275-89. doi: 10.1002/(sici)1097-4644(199608)62:2<275::aid-jcb15>3.0.co;2-k.
The nuclear matrix is the structure that persists after removal of chromatin and loosely bound components from the nucleus. It consists of a peripheral lamina-pore complex and an intricate internal fibrogranular structure. Little is known about the molecular structure of this proteinaceous internal network. Our aim is to identify the major proteins of the internal nuclear matrix of HeLa 53 cells. To this end, a cell fraction containing the internal fibrogranular structure was compared with one from which this structure had been selectively dissociated. Protein compositions were quantitatively analyzed after high-resolution two-dimensional gel electrophoresis. We have identified the 21 most abundant polypeptides that are present exclusively in the internal nuclear matrix. Sixteen of these proteins are heterogeneous nuclear ribonucleoprotein (hnRNP) proteins. B23 (numatrin) is another abundant protein of the internal nuclear matrix. Our results show that most of the quantitatively major polypeptides of the internal nuclear matrix are proteins involved in RNA metabolism, including packaging and transport of RNA.
核基质是在从细胞核中去除染色质和松散结合的成分后仍然存在的结构。它由外周板层-孔复合体和复杂的内部纤维颗粒结构组成。关于这种蛋白质内部网络的分子结构知之甚少。我们的目标是鉴定HeLa 53细胞内核基质的主要蛋白质。为此，将含有内部纤维颗粒结构的细胞组分与该结构已被选择性解离的组分进行比较。在高分辨率二维凝胶电泳后对蛋白质组成进行定量分析。我们已经鉴定出仅存在于内核基质中的21种最丰富的多肽。这些蛋白质中有16种是不均一核核糖核蛋白（hnRNP）。B23（核基质素）是内核基质的另一种丰富蛋白质。我们的结果表明，内核基质中大多数定量主要多肽是参与RNA代谢的蛋白质，包括RNA的包装和运输。
