Indirect DNA Readout by an H-NS Related Protein: Structure of the DNA Complex of the C-Terminal Domain of Ler

@inproceedings{Cordeiro2011IndirectDR,
  title={Indirect DNA Readout by an H-NS Related Protein: Structure of the DNA Complex of the C-Terminal Domain of Ler},
  author={Tiago N. Cordeiro and Holger Schmidt and Cristina Madrid and Antonio Ju{\'a}rez and Pau Bernad{\'o} and Christian Griesinger and Jes{\'u}s Garc{\'i}a and Miquel Pons},
  booktitle={PLoS pathogens},
  year={2011}
}
Ler, a member of the H-NS protein family, is the master regulator of the LEE pathogenicity island in virulent Escherichia coli strains. Here, we determined the structure of a complex between the DNA-binding domain of Ler (CT-Ler) and a 15-mer DNA duplex. CT-Ler recognizes a preexisting structural pattern in the DNA minor groove formed by two consecutive regions which are narrower and wider, respectively, compared with standard B-DNA. The compressed region, associated with an AT-tract, is sensed… CONTINUE READING

Citations

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Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

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