Circular dichroism, thermal denaturation, and deoxyribonuclease I digestion studies of nucleosomes highly enriched in high mobility group proteins HMG 1 and HMG 2.
Circular dichroism, thermal denaturation, and deoxyribonuclease I digestion studies of nucleosomes highly enriched in high mobility group proteins HMG 1 and HMG 2.
复制标题
高富集高迁移率基团蛋白 HMG 1 和 HMG 2 的核小体的圆二色性、热变性和脱氧核糖核酸酶 I 消化研究。
DOI:
10.1021/bi00507a060
复制
发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Rill,RL
中科院分区:
文献类型:
--
作者:
Jackson,JB;Rill,RL
James B. Jackson* and Randolph L. Rill* abstract: Salt-soluble (S) nucleosomes that contain near equimolar high mobility group nonhistone chromosomal proteins HMG 1 and HMG 2 and lack histone HI were isolated from mouse myeloma nuclei. Comparisons of the sedimen-tation, near-UV circular dichroism, thermal denaturation, and pattern of DNase I digestion of S nucleosomes with these properties of nucleosome cores or “typical” nucleosomes containing HI did not detect significant differences. These results indicate that HMG 1 and 2 do notaffect the confer-va have recently described the isolation of an unusual subset of nucleosomes that are released from mouse myeloma nuclei under near-physiological ionic conditions after very slight treatment with micrococcal nuclease (Jackson et al., 1979). These nucleosomes contain an apparently normal complement of core histones (H2a, H2b, H3, H4) and ca. 200 bp1 length DNA, but lack histone HI, and instead contain near-stoichiometric amounts of two high mobility group nonhistone chromosomal proteins, HMG 1 and HMG 2. They are also enrichedin lesser amounts of several other nonhistone proteins.