Nucleosome-associated proteins and phosphoproteins of differentiating Friend erythroleukemia cells.

AUTOR(ES)

Neumann, J

RESUMO

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.

Documentos Relacionados

• Detection of glucocorticoid receptors on Friend erythroleukemia cells.
• Altered RNA/protein ratio associated with the induction of differentiation of Friend erythroleukemia cells.
• Localization of DNA methyltransferase in the chromatin of Friend erythroleukemia cells.
• Subcellular localization of the env-related glycoproteins in Friend erythroleukemia cells.
• Altered nucleosome spacing in newly replicated chromatin from Friend leukemia cells.