Hogan M E, Roberson M W, Austin R H
Center for Biotechnology, College of Medicine, Princeton University, NJ 08544.
Proc Natl Acad Sci U S A. 1989 Dec;86(23):9273-7. doi: 10.1073/pnas.86.23.9273.
In a previous experimental study, we proposed that the bending and torsional stiffness of DNA display a systematic sequence dependence. Subsequently, we developed an elastic strain model to quantify the sequence dependence of the bending and torsional rigidity in terms of nearest neighbor interactions and used that model to analyze the sequence dependence of the 434 repressor binding to its operator. The analysis presented here shows that, in the absence of significant local variation of DNA secondary structure, DNase I cleavage is strongly correlated with local variation in the bending flexibility as calculated from our elastic strain model and that the agreement is also quantitatively significant. It is proposed that analysis using elastic strain models will provide a preliminary set of biochemical and chemical tools to explore the relation between DNA flexibility and the binding of other proteins.
在之前的一项实验研究中,我们提出DNA的弯曲和扭转刚度呈现出系统的序列依赖性。随后,我们开发了一种弹性应变模型,以根据最近邻相互作用来量化弯曲和扭转刚度的序列依赖性,并使用该模型分析434阻遏蛋白与其操纵子结合的序列依赖性。此处给出的分析表明,在DNA二级结构不存在显著局部变化的情况下,DNase I切割与根据我们的弹性应变模型计算出的弯曲柔韧性的局部变化密切相关,并且这种一致性在数量上也很显著。有人提出,使用弹性应变模型进行分析将提供一套初步的生化和化学工具,以探索DNA柔韧性与其他蛋白质结合之间的关系。