Energetic coupling along an allosteric communication channel drives the binding of Jun-Fos heterodimeric transcription factor to DNA.
Energetic coupling along an allosteric communication channel drives the binding of Jun-Fos heterodimeric transcription factor to DNA.
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DOI：
10.1111/j.1742-4658.2011.08124.x
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发表时间：
2011-06
期刊：
影响因子：
--
通讯作者：
Farooq A
中科院分区：
文献类型：
--
作者：
Seldeen KL;Deegan BJ;Bhat V;Mikles DC;McDonald CB;Farooq A
Although allostery plays a central role in driving protein-DNA interactions, the physical basis of such cooperative behavior remains poorly understood. Herein, using isothermal titration calorimetry in conjunction with site-directed mutagenesis, we provide evidence that an intricate network of energetically-coupled residues within the basic regions of Jun-Fos heterodimeric transcription factor accounts for its allosteric binding to DNA. Remarkably, energetic coupling is prevalent in residues that are both close in space as well as residues distant in space, implicating the role of both short-range and long-range cooperative interactions in driving the assembly of this key protein-DNA interaction. Surprisingly, many of the energetically-coupled residues involved in orchestrating such a cooperative network of interactions are poorly conserved across other members of the bZIP family, underscoring the importance of basic residues in dictating the specificity of bZIP-DNA interactions. Collectively, our thermodynamic analysis maps an allosteric communication channel driving a key protein-DNA interaction central to cellular functions in health and disease.
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