PMID:3135462
| Citation |
Falconi, M, Gualtieri, MT, La Teana, A, Losso, MA and Pon, CL (1988) Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS. Mol. Microbiol. 2:323-9 |
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| Abstract |
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. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins; DNA-Binding Proteins; Dimethyl Adipimidate; Dimethyl Suberimidate; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Macromolecular Substances; Molecular Sequence Data; Protein Conformation |
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