Indirect recognition in sequence-specific DNA binding by Escherichia coli integration host factor: the role of DNA deformation energy.

@article{Aeling2006IndirectRI,
  title={Indirect recognition in sequence-specific DNA binding by Escherichia coli integration host factor: the role of DNA deformation energy.},
  author={Kimberly A. Aeling and Michael L. Opel and Nicholas R. Steffen and Vira Tretyachenko-Ladokhina and G. Wesley Hatfield and Richard H. Lathrop and Donald F. Senear},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 51},
  pages={39236-48}
}
Integration host factor (IHF) is a bacterial histone-like protein whose primary biological role is to condense the bacterial nucleoid and to constrain DNA supercoils. It does so by binding in a sequence-independent manner throughout the genome. However, unlike other structurally related bacterial histone-like proteins, IHF has evolved a sequence-dependent, high affinity DNA-binding motif. The high affinity binding sites are important for the regulation of a wide range of cellular processes. A… CONTINUE READING
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