Nucleosome-associated proteins and phosphoproteins of differentiating Friend erythroleukemia cells.
Mononucleosomes derived from brief digestion of uninduced Friend cell nuclei with micrococcal nuclease contain a set of non-histone chromosomal proteins which are partly or altogether missing in the oligomeric nucleosomes. On the other hand, the latter contain a protein of Mr 190,000 not seen in the mononucleosomes. Longer digestion removes most of these non-histone proteins, excepting the Mr 190,000 protein. Brief digestion of nuclei from Friend cells induced by DMSO or by n-butyrate removes most of the non-histone proteins from the nucleosomes, as did the prolonged digestion of uninduced nuclei. The Mr 190,000 protein remains, while a protein of Mr 27,000 is increased. The rate of phosphorylation of histone H1 associated with mononucleosomes was 3 to 4-fold greater in cells induced with DMSO. The major phosphoprotein and most of the other phosphorylated non-histones were modified at the same rate in control and induced cells. However, a Mr 95,000 protein was less phosphorylated in the induced cells.
D000818:Animals; D002454:Cell Differentiation; D002460:Cell Line; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis; D005622:Friend murine leukemia virus; D007942:Leukemia, Experimental; D008970:Molecular Weight; D009698:Nucleoproteins / Q000032:analysis*; D010750:Phosphoproteins / Q000032:analysis*
D002868:Chromosomal Proteins, Non-Histone; D009698:Nucleoproteins; D010750:Phosphoproteins