Binding of histones H1 and H5 and their globular domains to four-way junction DNA.
Binding of histones H1 and H5 and their globular domains to four-way junction DNA.
复制标题
组蛋白 H1 和 H5 及其球状结构域与四路连接 DNA 的结合。
DOI：
10.1073/pnas.91.9.3525
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发表时间：
1994
影响因子：
11.1
通讯作者：
vanHolde,K
中科院分区：
文献类型：
--
作者：
Varga-Weisz,P;Zlatanova,J;Leuba,SH;Schroth,GP;vanHolde,K
我们比较了鸡红细胞接头组蛋白H1和H5结合到一个合成的四路DNA连接。每个组蛋白结合形成单个复合物，其亲和力允许与大量过量的线性双链DNA竞争。H5的亲和力高于H1。来自任一蛋白质的球状结构域也将强烈结合，但在这种情况下发生多重结合。完整的H1的结合被阳离子抑制：Mg 2+和亚精胺是非常有效的，Na+少得多。这种抑制不太可能是一般的离子竞争效应，因为Mg 2+在抑制H1与线性DNA结合方面的效果要小得多。相反，结合的抑制可能是由于四向连接的构象的离子依赖性变化，这是已知的发生在类似的条件下。这些结果有力地表明，DNA连接臂之间形成的角度可能是H1与DNA交叉相互作用的主要决定因素。
We have compared chicken erythrocyte linker histones H1 and H5 binding to a synthetic four-way DNA junction. Each histone binds to form a single complex, with an affinity which permits competition against a large excess of linear duplex DNA. The affinity of H5 is higher than that of H1. The globular domain from either protein will also bind strongly, but in this case multiple binding occurs. Binding of intact H1 is inhibited by cations: Mg2+ and spermidine are very effective, Na+ much less so. This inhibition is not likely to be a general ion-competition effect, for Mg2+ is much less effective in inhibiting the binding of H1 to linear DNA. Instead, the inhibition of binding may be due to ion-dependent changes in the conformation of the four-way junction, which are known to occur under similar conditions. These results strongly suggest that the angle formed between the arms of the DNA junction could be a major determinant in the interaction of H1 with DNA crossovers.
影响因子：
4.3
作者：
H. Sambrook
通讯作者：
H. Sambrook
鸡红细胞核的组蛋白。
DOI：
--
发表时间：
1964
期刊：
Canadian Journal of Biochemistry
影响因子：
--
作者：
J. M. Neelin;P. Callahan;D. Lamb;K. Murray
通讯作者：
K. Murray