Sandeen G, Wood W I, Felsenfeld G
Nucleic Acids Res. 1980 Sep 11;8(17):3757-78. doi: 10.1093/nar/8.17.3757.
The interaction of the high mobility group proteins, HMG14 and HMG17, with nucleosome core particles has been studied. The results show that two molecules of HMG14/17 can be bound tightly but reversibly to each core particle and that their affinity for core particles is greater than their affinity for histone-free DNA of core size. Thermal denaturation and nuclease digestion studies suggest that major sites of interaction are located near the ends of the nucleosome core DNA. When nucleosome preparations from chicken erythrocyte nuclei stripped of HMG proteins are partially titrated with HMG14/17, the nucleosome-HMG complex fraction is enriched in beta-globin gene sequences.
对高迁移率族蛋白HMG14和HMG17与核小体核心颗粒的相互作用进行了研究。结果表明,两分子的HMG14/17能紧密但可逆地结合到每个核心颗粒上,并且它们对核心颗粒的亲和力大于对核心大小的无组蛋白DNA的亲和力。热变性和核酸酶消化研究表明,主要的相互作用位点位于核小体核心DNA的末端附近。当用HMG14/17对从鸡红细胞核中去除HMG蛋白的核小体制剂进行部分滴定后,核小体-HMG复合组分富含β-珠蛋白基因序列。