Characterization of lamina-bound chromatin in the nuclear shell isolated from HeLa cells.
The structure and the polypeptide composition of the nuclear shell isolated from interphase HeLa cells have been investigated and compared to those of the intranuclear material. The isolated nuclear shell contains chromatin superstructures (28-32 nm thick fibres) made of tightly packed nucleosomes that resist low ionic strength conditions and that are associated with the three nuclear lamins. Chromatin in the nuclear shell exhibits very simple chemical composition. Especially, non-histone proteins are lacking. The results presented here rule out the possibility that the nuclear shell results from contamination of lamina by intranuclear elements. They suggest that the lamins are directly involved in the specific properties and in the organization of chromatin in the nuclear shell.
D002458:Cell Fractionation; D002467:Cell Nucleus / Q000032:analysis; D002843:Chromatin / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis; D006367:HeLa Cells; D006609:High Mobility Group Proteins / Q000032:analysis; D006657:Histones / Q000032:analysis*; D006801:Humans; D034882:Lamins; D008854:Microscopy, Electron; D009685:Nuclear Envelope / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D009698:Nucleoproteins / Q000032:analysis*; D009707:Nucleosomes / Q000648:ultrastructure; D012261:Ribonucleoproteins / Q000032:analysis
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D006609:High Mobility Group Proteins; D006657:Histones; D034882:Lamins; D009698:Nucleoproteins; D009707:Nucleosomes; D012261:Ribonucleoproteins