Gal repressosome contains an antiparallel DNA loop

Nat Struct Biol. 2001 May;8(5):432-6. doi: 10.1038/87595.

Abstract

Gal repressosome assembly and repression of the gal operon in Escherichia coli occurs when two dimeric GalR proteins and the histone-like HU protein bind to cognate sites causing DNA looping. Structure-based genetic analysis defined the GalR surfaces interacting to form a stacked, V-shaped, tetrameric structure. Stereochemical models of the four possible DNA loops compatible with the GalR tetramer configuration were constructed using the sequence-dependent structural parameters of the interoperator DNA and conformation changes caused by GalR and asymmetric HU binding. Evaluation of their DNA elastic energies gave unambiguous preference to a loop structure in which the two gal operators adopt an antiparallel orientation causing undertwisting of DNA.

MeSH terms

  • Amino Acid Substitution / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • DNA, Bacterial / chemistry*
  • DNA, Bacterial / genetics
  • DNA, Bacterial / metabolism*
  • DNA-Binding Proteins / metabolism
  • Dimerization
  • Elasticity
  • Escherichia coli Proteins
  • Escherichia coli* / chemistry
  • Escherichia coli* / genetics
  • Kinetics
  • Models, Molecular
  • Mutation / genetics
  • Nucleic Acid Conformation*
  • Operon / genetics
  • Protein Structure, Quaternary
  • Repressor Proteins / chemistry
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*
  • Structure-Activity Relationship
  • Thermodynamics

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Galactose repressor proteins
  • Repressor Proteins
  • histone-like protein HU, bacteria