Effect of HMG protein 17 on the thermal stability of control and acetylated HeLa oligonucleosomes.
Effect of HMG protein 17 on the thermal stability of control and acetylated HeLa oligonucleosomes.
复制标题
HMG 蛋白 17 对对照和乙酰化 HeLa 寡核小体热稳定性的影响。
DOI：
10.1093/nar/11.9.2651
复制
发表时间：
1983
影响因子：
14.9
通讯作者：
Bradbury,EM
中科院分区：
文献类型：
--
作者：
Yau,P;Imai,BS;Thorne,AW;Goodwin,GH;Bradbury,EM
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.
