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Nucleic Acids Research, 1988, Vol. 16, No. 13 5915-5926
© 1988

Articles

Erythroid-specific gene chromatin has an altered association with linker histones

J.A. Ridsdale, J.B. Rattner1 and J. R. Davie

Department of Biochemistry, University of Manitoba 770 Bannatyne Avenue, Winnipeg, Manitoba, R3E OW3, Canada 1Department of Anatomy and Cell Biology, University of Calgary Calgary, Alberta T2N 4N1, Canada

Received March 23, 1988. Revised May 24, 1988. Accepted May 24, 1988.

The chromatin of several genes was assayed for sensitivity to DNAase I and for solubility as polynucleosomes in 0.15 M NaCl. The degree of solubility of chromatin fragments as polynucleosomes in 0.15 M Nad correlates well with the sensitivity to DNAase I for several genes. Chromatin of repressed, housekeeping and erythroid-specific genes can be distinguished as distinct groups by the degree to which they display these properties. NaCl precipitation of chromatin fragments stripped and then reconstituted with varying quantities of H1 and H5 (linker) histones indicate that the polynucleosomes of erythroid-specific genes have altered interaction with these histones. Linker histones interacted with bulk chromatin and in the chromatin of the repressed ovalbumin and vitellogenin genes to form salt precipitable structures. Chromatin of erythroid-specific genes (histone H5 and ß-globin) as well as that of the histone H2A.F gene was resistant to linker histone induced precipitation.


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