hnRNP proteins and B23 are the major proteins of the internal nuclear matrix of HeLa S3 cells

• Published in: Journal of cellular biochemistry Vol. 62; no. 2; pp. 275 - 289
• Main Authors: Mattern, Karin A., Humbel, Bruno M., Muijsers, Anton O., Jong, Luitzen de, Driel, Roel van
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01-08-1996
• Subjects: 2-D gel electrophoresis; B23; Cell Fractionation; Cell Nucleus - chemistry; Electrophoresis, Gel, Two-Dimensional; HeLa Cells - chemistry; HeLa S3 cells; Heterogeneous-Nuclear Ribonucleoproteins; Humans; nuclear matrix; Nuclear Matrix - chemistry; Nuclear Matrix - ultrastructure; Nuclear Proteins - analysis; Ribonucleoproteins - analysis; Vimentin - analysis
• ISSN: 0730-2312; 1097-4644
• 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 S3 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. © 1996 Wiley‐Liss, Inc.