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A high-throughput percentage-of-binding strategy to measure binding energies in DNA-protein interactions: application to genome-scale site discovery.


ABSTRACT: Quantifying the binding energy in DNA-protein interactions is of critical importance to understand transcriptional regulation. Based on a simple computational model, this study describes a high-throughput percentage-of-binding strategy to measure the binding energy in DNA-protein interactions between the Shewanella oneidensis ArcA two-component transcription factor protein and a systematic set of mutants in an ArcA-P (phosphorylated ArcA) binding site. The binding energies corresponding to each of the 4 nt at each position in the 15-bp binding site were used to construct a position-specific energy matrix (PEM) that allowed a reliable prediction of ArcA-P binding sites not only in Shewanella but also in related bacterial genomes.

SUBMITTER: Wang X 

PROVIDER: S-EPMC2528174 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature

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A high-throughput percentage-of-binding strategy to measure binding energies in DNA-protein interactions: application to genome-scale site discovery.

Wang Xiaohu X   Gao Haichun H   Shen Yufeng Y   Weinstock George M GM   Zhou Jizhong J   Palzkill Timothy T  

Nucleic acids research 20080724 15


Quantifying the binding energy in DNA-protein interactions is of critical importance to understand transcriptional regulation. Based on a simple computational model, this study describes a high-throughput percentage-of-binding strategy to measure the binding energy in DNA-protein interactions between the Shewanella oneidensis ArcA two-component transcription factor protein and a systematic set of mutants in an ArcA-P (phosphorylated ArcA) binding site. The binding energies corresponding to each  ...[more]

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