大肠杆菌DNA结合蛋白与核酸之间相互作用的物理学研究。
Physical studies of the interaction between the Escherichia coli DNA binding protein and nucleic acids.
作者信息
Molineux I J, Pauli A, Gefter M L
出版信息
Nucleic Acids Res. 1975 Oct;2(10):1821-37. doi: 10.1093/nar/2.10.1821.
Abstract
The interaction of nucleic acid with the Escherichia coli DNA-binding protein has been studied by fluorescence emission spectroscopy and sedimentation velocity analysis. The protein binds to single-strand DNA with an apparent equilibrium dissociation constant of 2 X 10(-9). It binds to the homopolymers poly (dA) and poly (dT) slightly more tightly, but has a larger apparent equilibrium dissociation constant to poly (dC). The protein also binds tightly to ribohomopolymers and to tRNA, but not to duplex DNA. By the use of defined-length oligonucleotides, it has been shown that the protein binds to DNA in a highly cooperative manner. The extent of cooperativity is seen as the difference in binding between an isolated monomeric protein molecule bound to DNA and two or more molecules binding to contiguous sites.
摘要
通过荧光发射光谱和沉降速度分析研究了核酸与大肠杆菌DNA结合蛋白的相互作用。该蛋白与单链DNA结合，表观平衡解离常数为2×10⁻⁹。它与同聚物聚（dA）和聚（dT）的结合稍紧密一些，但与聚（dC）的表观平衡解离常数更大。该蛋白也与核糖同聚物和tRNA紧密结合，但不与双链DNA结合。通过使用确定长度的寡核苷酸，已表明该蛋白以高度协同的方式与DNA结合。协同程度表现为与DNA结合的孤立单体蛋白分子和与相邻位点结合的两个或更多分子之间结合的差异。
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