Nucleic Acids Research, 1983, Vol. 11, No. 9 2651-2664
© 1983
MOLECULAR BIOLOGY |
Effect of HMG protein 17 on tbe thermal stability of control and acetylated HeLa oligonadeosomes
Department of Biological Chemistry, School of Medicine, University of California Davis, CA 95616, USA *Institute of Cancer Research, Royal Cancer Hospital, Chester Beatty Research Institute Fulham Road, London SW3 6JB, UK
Received February 9, 1983. Revised March 29, 1983. Accepted March 29, 1983.
Many studies have implicated histone acetylation and HMG proteins 14 and 17 in the structure of active chromatin. Studies of the binding of HMG 14 and 17 to chromatin core particles have shown that there are two binding sites for HMG 14 or 17 located vnthin 20–25 bp of the DNA ends of the core particles [13–15]. Such binding sites may result from the free DNA ends in the core particle being available for the binding of HMG 14 and 17. We have studied the effects of the binding of HMG 17 on the thermal denaturation of DNA 1n mono, d1 and trinucleosomes. In each case the binding of 1 HMG 17 molecule per nucleosome reduces the DNA premelt region by 50%, while the binding of 2 HMG 17 molecules per nucleosome abolishes the premelt region. From this it 1s concluded that there are two HMG 17 binding sites per nucleosome which are located between the entry and exit points to the nucleosome and the strongly complexed central DNA region. Highly acetylated mono, di and trinucleosomes have been isolated from butyrate treated HeLa S3 cells. For this series of acetylated oligonucleo-somes, 1t has been found that there are also two HMG 17 binding sites per acetylated nucleosome.
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