INTERACTIONS OF A PURIFIED NON-HISTONE CHROMOSOMAL PROTEIN WITH DNA AND HISTONE

INTERACTIONS OF A PURIFIED NON-HISTONE CHROMOSOMAL PROTEIN WITH DNA AND HISTONE
复制标题

DOI:
10.1111/j.1432-1033.1974.tb03690.x
复制
发表时间:
1974-01-01
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
通讯作者:
JOHNS, EW
JOHNS, EW
中科院分区:
其他
文献类型:
--
作者:
SHOOTER, KV;GOODWIN, GH;JOHNS, EW

文献摘要

被引文献

相似文献

1.通过超离心沉降分析研究了纯化的小牛胸腺染色体非组蛋白蛋白(命名为HMG 1蛋白)与噬菌体T7 DNA和小牛胸腺DNA的相互作用。所得结果表明:(a)非组蛋白HMG 1以离子强度依赖性方式与DNA结合,(B)DNA可结合高达其重量约4 - 5倍的HMG 1蛋白,该蛋白自身沿着DNA链均匀分布,以及(c)相互作用是快速可逆平衡。这些结果被解释为表明蛋白质HMG 1通过蛋白质的碱性氨基酸和DNA的磷酸基团之间的离子键合与DNA结合。平衡沉降研究进行了蛋白质HMG 1和组蛋白F1的混合物。结果表明,HMG 1蛋白与组蛋白F1.3结合。用平衡沉降法测定了HMG 1蛋白的分子量,其平均值为26500。
1. The interactions of a purified calf thymus chromosomal non‐histone protein (designated protein HMG1) with bacteriophage T7 DNA and calf thymus DNA have been investigated by sedimentation analysis in the ultracentrifuge. The results obtained show that (a) the non‐histone protein HMG1 binds to DNA in an ionic‐strength‐dependent manner, (b) the DNA can bind up to approximately four to five times its weight of protein HMG1, the protein distributing itself evenly along the DNA chains, and (c) the interaction is a rapid reversible equilibrium. These results are interpreted as indicating that protein HMG1 binds to DNA through ionic bonding between the basic amino acids of the protein and the phosphate groups of the DNA.2. Equilibrium sedimentation studies were carried out on mixtures of protein HMG1 and histone F1. The results demonstrate that protein HMG1 combines with histone F1.3. The molecular weight of protein HMG1 has been determined by equilibrium sedimentation and a mean value of 26500 was obtained.