The architecture of ArgR-DNA complexes at the genome-scale in Escherichia coli

Nucleic Acids Res. 2015 Mar 31;43(6):3079-88. doi: 10.1093/nar/gkv150. Epub 2015 Mar 3.

Abstract

DNA-binding motifs that are recognized by transcription factors (TFs) have been well studied; however, challenges remain in determining the in vivo architecture of TF-DNA complexes on a genome-scale. Here, we determined the in vivo architecture of Escherichia coli arginine repressor (ArgR)-DNA complexes using high-throughput sequencing of exonuclease-treated chromatin-immunoprecipitated DNA (ChIP-exo). The ChIP-exo has a unique peak-pair pattern indicating 5' and 3' ends of ArgR-binding region. We identified 62 ArgR-binding loci, which were classified into three groups, comprising single, double and triple peak-pairs. Each peak-pair has a unique 93 base pair (bp)-long (±2 bp) ArgR-binding sequence containing two ARG boxes (39 bp) and residual sequences. Moreover, the three ArgR-binding modes defined by the position of the two ARG boxes indicate that DNA bends centered between the pair of ARG boxes facilitate the non-specific contacts between ArgR subunits and the residual sequences. Additionally, our approach may also reveal other fundamental structural features of TF-DNA interactions that have implications for studying genome-scale transcriptional regulatory networks.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Binding Sites / genetics
  • Chromatin Immunoprecipitation
  • DNA, Bacterial / chemistry
  • DNA, Bacterial / genetics*
  • DNA, Bacterial / metabolism*
  • DNA-Directed RNA Polymerases / metabolism
  • Escherichia coli K12 / genetics*
  • Escherichia coli K12 / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism*
  • Genome, Bacterial
  • High-Throughput Nucleotide Sequencing
  • Macromolecular Substances / chemistry
  • Macromolecular Substances / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Quaternary
  • Repressor Proteins / chemistry
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*

Substances

  • ArgR protein, E coli
  • DNA, Bacterial
  • Escherichia coli Proteins
  • Macromolecular Substances
  • Repressor Proteins
  • DNA-Directed RNA Polymerases

Associated data

  • GEO/GSE60546