The interaction of core histones with DNA: equilibrium binding studies.
The interaction of core histones with DNA: equilibrium binding studies.
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核心组蛋白与 DNA 的相互作用：平衡结合研究。
DOI：
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发表时间：
1978
影响因子：
14.9
通讯作者：
I. O. Walker
中科院分区：
文献类型：
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作者：
Dennis R. Burton;M. J. Butler;John E. Hyde;D. Phillips;C. Skidmore;I. O. Walker
核心组蛋白与DNA的结合是一个可逆的过程，以[NaCl]的函数来测量。解离和再结合发生在两个阶段。在0.7 ~ 1.2 M NaCl条件下，H2a和H2b在4℃和1.0 M NaCl条件下以δ ago = 1.6 kcal /mol的等摩尔配合物非协同结合。在1.2 ~ 2.0 M NaCl条件下，H3和H4在4℃和1.0 M NaCl条件下形成等摩尔配合物，δ Go = 7.4 Kcal/mol。H2a和H2b的正确结合需要结合的H3和H4的存在。核酸酶对H3-H4 DNA的酶切产生一个H3-H4的四聚体，它与145、125和104碱基对长的DNA片段结合。因此，H3-H4四聚体可以保护DNA片段，只要这些片段存在于完整的核小体核心颗粒中，因此必须跨越核小体核心颗粒。
The binding of core histone proteins to DNA, measured as a function of [NaCl[ is a reversible process. Dissociation and reassociation occurs in two stages. Between 0.7 and 1.2 M NaCl H2a H2b bind non-cooperatively as an equimolar complex with deltaGo = 1.6 Kcals/mole at 4 degree C and 1.0 M NaCl. Between 1.2 and 2.0 M NaCl H3 and H4 bind cooperatively as an equimolar complex with delta Go = 7.4 Kcal/mole at 4 degree C and 1.0 M NaCl. The proper binding of H2a and H2b requires the presence of bound H3 and H4. Nuclease digestion of the H3-H4 DNA produces a tetramer of H3-H4 bound to fragments of DNA 145, 125 and 104 base pairs long. Thus an H3-H4 tetramer can protect fragments of DNA as long as those found in complete core particles and must therefore span the nucleosome core particle.