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hnRNP proteins and B23 are the major proteins of the internal nuclear matrix of HeLa S3 cells
Author(s) -
Mattern Karin A.,
Humbel Bruno M.,
Muijsers Anton O.,
Jong Luitzen de,
Driel Roel van
Publication year - 1996
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(199608)62:2<275::aid-jcb15>3.0.co;2-k
Subject(s) - nuclear matrix , nuclear lamina , nuclear protein , heterogeneous nuclear ribonucleoprotein , chromatin , cell nucleus , rna , hela , microbiology and biotechnology , ribonucleoprotein , matrix (chemical analysis) , nuclear pore , chemistry , nucleoporin , nucleus , biology , nuclear transport , biochemistry , biophysics , cell , dna , gene , transcription factor , chromatography
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.