Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS

Mol Microbiol. 1988 May;2(3):323-9. doi: 10.1111/j.1365-2958.1988.tb00035.x.


The primary sequence of H-NS (136 amino acid residues, Mr = 15,402), an abundant Escherichia coli DNA-binding protein, has been elucidated and its quaternary structure has been investigated by protein-protein cross-linking reactions. It was found that H-NS exists predominantly as a dimer, even at very low concentrations, but may form tetramers at higher concentrations and that the protein-protein interaction responsible for the dimerization is chiefly hydrophobic.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • DNA-Binding Proteins*
  • Dimethyl Adipimidate
  • Dimethyl Suberimidate
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli*
  • Macromolecular Substances
  • Molecular Sequence Data
  • Protein Conformation


  • Bacterial Proteins
  • DNA-Binding Proteins
  • H-NS protein, bacteria
  • Macromolecular Substances
  • Dimethyl Adipimidate
  • Dimethyl Suberimidate