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Nucleic Acids Research, 1979, Vol. 7, No. 7 1815-1835
© 1979

Articles

Analysis of the high mobility group proteins associated with salt-soluble nucleosomes

Graham H. Goodwin*, Christopher G.P. Mathew*, Carol A. Wright*, Christo D. Venkov** and Ernest W. Johns*

*Chester Beatty Research Institute, Institute of Cancer Research, Royal Cancer Hospital Fulham Road, London SW3, UK, **Institute of Molecular Biology, Bulgarian Academy of Sciences 1113 Sofia, Bulgaria

Received October 1, 1979. Two methods have recently been described for the isolation of monomer nucleosomes enriched in transcribed sequences which depend on their solubility in 0.1 M NaCl (Levy, W.B. and Dixon (1978), Nucleic Acid Res., 5, 4155-4163) or solutions containing divalent metal ions (Bloom, K.S. and Anderson, J.N. (1978), Cell, 15, 141–150). Using these procedures the proteins associated with such nucleosomes from rabbit thyraus, calf liver and hen oviduct nuclei were isolated and analysed. Increased amounts of proteins HMG14 and HMG17 and small amounts of HMG1 and HMG2 were found associated with the four core histones H2A, H2B, H3 and H4 in these nucleosomes. HMG14 and HMG17 were found to be enriched 2–7 fold, suggesting an involvement of these two proteins with transcribed sequences.

0.1 M NaCl-soluble monomer nucleosomes prepared by the method of Levy and Dixon were analysed by polyacrylamide gel electrophoresis and found to be composed of principally two types of particle:

1. Core particles of 145 base pairs of DNA associated with the four core hiatones only.

2. Nucleosomes with 160 base pairs of DNA associated with the four core histones, increased amounts of HMG14 and 17, and no HI. Small amounts of HMG1 and HMG2 are also detected.

These results suggest that HMG14 and HMG17 might be interacting with the 15 base pair linker DNA. A model is presented for the structure of transcriptionally active chromatin.


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