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The H-NS dimerization domain defines a new fold contributing to DNA recognition
- Source :
- Nature Structural Biology, Nature Structural Biology, Nature Publishing Group, 2003, 10 (3), pp.212-8. 〈10.1038/nsb904〉, Nature Structural Biology, Nature Publishing Group, 2003, 10 (3), pp.212-8. ⟨10.1038/nsb904⟩, Nature Structural Biology, 2003, 10 (3), pp.212-8. ⟨10.1038/nsb904⟩
- Publication Year :
- 2003
- Publisher :
- HAL CCSD, 2003.
-
Abstract
- International audience; 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.
- Subjects :
- Models, Molecular
Protein Folding
Magnetic Resonance Spectroscopy
MESH : Molecular Sequence Data
Protein Conformation
MESH : DNA
MESH: Amino Acid Sequence
MESH: Protein Structure, Tertiary
chemistry.chemical_compound
MESH: Protein Conformation
Structural Biology
MESH : Bacterial Proteins
MESH: Peptide Fragments
MESH: Bacterial Proteins
Conserved Sequence
MESH : Protein Conformation
0303 health sciences
MESH: Conserved Sequence
MESH : Amino Acid Sequence
MESH: DNA
DNA-Binding Proteins
Biochemistry
MESH : Dimerization
MESH : DNA-Binding Proteins
MESH : Mutation
Dimerization
MESH : Protein Structure, Tertiary
MESH: Models, Molecular
Binding domain
MESH : Protein Folding
MESH: Mutation
HMG-box
MESH : Models, Molecular
MESH: Protein Folding
Molecular Sequence Data
Fluorescence Polarization
Computational biology
Biology
DNA-binding protein
03 medical and health sciences
Bacterial Proteins
MESH : Conserved Sequence
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Amino Acid Sequence
B3 domain
Molecular Biology
Gene
[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology
030304 developmental biology
MESH: Fluorescence Polarization
MESH: Molecular Sequence Data
MESH: Magnetic Resonance Spectroscopy
030306 microbiology
Circular bacterial chromosome
MESH : Peptide Fragments
DNA
Peptide Fragments
Protein Structure, Tertiary
MESH: Dimerization
Heteronuclear molecule
chemistry
Mutation
MESH : Fluorescence Polarization
MESH : Magnetic Resonance Spectroscopy
MESH: DNA-Binding Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 10728368
- Database :
- OpenAIRE
- Journal :
- Nature Structural Biology, Nature Structural Biology, Nature Publishing Group, 2003, 10 (3), pp.212-8. 〈10.1038/nsb904〉, Nature Structural Biology, Nature Publishing Group, 2003, 10 (3), pp.212-8. ⟨10.1038/nsb904⟩, Nature Structural Biology, 2003, 10 (3), pp.212-8. ⟨10.1038/nsb904⟩
- Accession number :
- edsair.doi.dedup.....a979357996c73c86a439136443f31bdf