Protein-induced DNA bending clarifies the architectural organization of the sigma54-dependent glnAp2 promoter.

@article{Huo2006ProteininducedDB,
  title={Protein-induced DNA bending clarifies the architectural organization of the sigma54-dependent glnAp2 promoter.},
  author={Yi-Xin Huo and Zhe-Xian Tian and Mathieu Rappas and Jin Wen and Yan-Cheng Chen and Cong-Hui You and Xiaodong Zhang and Martin Buck and Yiping Wang and Annie Kolb},
  journal={Molecular microbiology},
  year={2006},
  volume={59 1},
  pages={168-80}
}
Sigma54-RNA polymerase (Esigma54) predominantly contacts one face of the DNA helix in the closed promoter complex, and interacts with the upstream enhancer-bound activator via DNA looping. Up to date, the precise face of Esigma54 that contacts the activator to convert the closed complex to an open one remains unclear. By introducing protein-induced DNA bends at precise locations between upstream enhancer sequences and the core promoter of the sigma54-dependent glnAp2 promoter without changing… CONTINUE READING

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