Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS.
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.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D004119:Dimethyl Adipimidate; D004120:Dimethyl Suberimidate; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011487:Protein Conformation
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C031908:H-NS protein, bacteria; D046911:Macromolecular Substances; D004119:Dimethyl Adipimidate; D004120:Dimethyl Suberimidate