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 = 15402), 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.

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