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Nucleic Acids Research, 1978, Vol. 5, No. 5 1675-1687
© 1978

Articles

Nucleosome-associated proteins and phosphoproteins of differentiating Friend erythroleukemia cells

Jeffrey Neumann, Robert Whittaker*, Barbara Blanchard and Vernon Ingram

Department of Biology, Massachusetts Institute of Technology Cambridge, MA 02139, USA

Received March 8, 1978.

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.

*Present address: Genetics Research Laboratories, North Ryde, P. O. Box 184, North Ryde, N.S.W., 2113, N.S.W. Australia 2121.


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