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Nucleic Acids Research, 1985, Vol. 13, No. 10 3561-3579
© 1985

Articles

The effect of salt extraction on the structure of transcriptionally active genes; evidence for a DNAseI-sensitive structure which could be dependent on chromatin structure at levels higher than the 30 nm fibre

G. H. Goodwin, R. H. Nicolas, P. N. Cockerill, S. Zavou and C. A. Wright

Institute of Cancer Research, Royal Marsden Hospital, Chester Beatty Laboratories Fulham Road, London SW3 6JB, UK

Received November 27, 1984. Revised April 21, 1985. Accepted April 21, 1985.

The procedure developed by Lawson and Cole (Biochemistry, 1979, 18 2161–2166) for removing lysine-rich histones from nuclei at low pH also quantitatively extracts proteins HMG14 and 17. The effect of this low pH extraction on the DNAseI-sensitive structures of active genes in avian red blood cells has been investigated. No major perturbation of a developtnentally regulated DNAseI hypersensitive site in the ß-globin domain and at the 5' end of the {alpha}D gene was seen. The overall DNAseI-sensitive conformation of the BA-globin gene (relative to the ovalbumin gene) is minimally affected by pH3 salt extraction, but there is some loss of sensitivity of the {alpha}D gene. Removal of HMG proteins at neutral pH had no effect on the sensitivity of active genes in erythroid or fibroblast nuclei. These results, together with those carried out on DNAseI sensitivity and HMG binding to monomer nucleosomes, indicate that there is a major structural feature of active genes responsible for DNAseI-sensitivity which is independent of HMG proteins or nucleosome core particle structure but may be dependent on higher order chromatin structures.


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