The H-NS dimerization domain defines a new fold contributing to DNA recognition
H-NS, a protein found in Gram-negative bacteria, is involved in structuring the bacterial chromosome and acts as a global regulator for the expression of a wide variety of genes. These functions are correlated with both its DNA-binding and oligomerization properties. We have identified the minimal d...
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| Veröffentlicht in: | Nature structural & molecular biology 2003-03, Vol.10 (3), p.212-218 |
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| container_title | Nature structural & molecular biology |
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| creator | Bloch, Vanessa Yang, Yinshan Margeat, Emmanuel Chavanieu, Alain Augé, Marie Thérèse Robert, Bruno Arold, Stefan Rimsky, Sylvie Kochoyan, Michel |
| description | H-NS, a protein found in Gram-negative bacteria, is involved in structuring the bacterial chromosome and acts as a global regulator for the expression of a wide variety of genes. These functions are correlated with both its DNA-binding and oligomerization properties. We have identified the minimal dimerization domain of H-NS, a 46 amino acid–long N-terminal fragment, and determined its structure using heteronuclear NMR spectroscopy. The highly intertwined structure of the dimer, reminiscent of a handshake, defines a new structural fold, which may offer a possibility for discriminating prokaryotic from eukaryotic proteins in drug design. Using mutational analysis, we also show that this N-terminal domain actively contributes to DNA binding, conversely to the current paradigm. Together, our data allows us to propose a model for the action of full length H-NS. |
| doi_str_mv | 10.1038/nsb904 |
| format | Article |
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These functions are correlated with both its DNA-binding and oligomerization properties. We have identified the minimal dimerization domain of H-NS, a 46 amino acid–long N-terminal fragment, and determined its structure using heteronuclear NMR spectroscopy. The highly intertwined structure of the dimer, reminiscent of a handshake, defines a new structural fold, which may offer a possibility for discriminating prokaryotic from eukaryotic proteins in drug design. Using mutational analysis, we also show that this N-terminal domain actively contributes to DNA binding, conversely to the current paradigm. 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These functions are correlated with both its DNA-binding and oligomerization properties. We have identified the minimal dimerization domain of H-NS, a 46 amino acid–long N-terminal fragment, and determined its structure using heteronuclear NMR spectroscopy. The highly intertwined structure of the dimer, reminiscent of a handshake, defines a new structural fold, which may offer a possibility for discriminating prokaryotic from eukaryotic proteins in drug design. Using mutational analysis, we also show that this N-terminal domain actively contributes to DNA binding, conversely to the current paradigm. 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| subjects | Amino Acid Sequence Amino acids Bacteria Bacterial Proteins Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry Biochemistry, Molecular Biology Biological Microscopy Biomedical and Life Sciences Conserved Sequence Deoxyribonucleic acid Dimerization DNA DNA - metabolism DNA-Binding Proteins DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Fluorescence Polarization Life Sciences Magnetic Resonance Spectroscopy Membrane Biology Models, Molecular Molecular Sequence Data Mutation Peptide Fragments Peptide Fragments - chemistry Protein Conformation Protein Folding Protein Structure Protein Structure, Tertiary |
| title | The H-NS dimerization domain defines a new fold contributing to DNA recognition |
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