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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... Full description

Journal Title: Nature structural & molecular biology 2003-03, Vol.10 (3), p.212-218
Main Author: Kochoyan, Michel
Other Authors: Bloch, Vanessa , Yang, Yinshan , Margeat, Emmanuel , Chavanieu, Alain , Augé, Marie Thérèse , Robert, Bruno , Arold, Stefan , Rimsky, Sylvie
Format: Electronic Article Electronic Article
Language: English
Subjects:
DNA
Quelle: Alma/SFX Local Collection
Publisher: United States: Nature Publishing Group
ID: ISSN: 1072-8368
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recordid: cdi_hal_primary_oai_HAL_hal_00257410v1
title: The H-NS dimerization domain defines a new fold contributing to DNA recognition
format: Article
creator:
  • Kochoyan, Michel
  • Bloch, Vanessa
  • Yang, Yinshan
  • Margeat, Emmanuel
  • Chavanieu, Alain
  • Augé, Marie Thérèse
  • Robert, Bruno
  • Arold, Stefan
  • Rimsky, Sylvie
subjects:
  • Amino Acid Sequence
  • Bacterial Proteins
  • Bacterial Proteins - chemistry
  • Bacterial Proteins - genetics
  • Bacterial Proteins - metabolism
  • Binding Proteins
  • Biochemistry
  • Biochemistry, Molecular Biology
  • Conserved Sequence
  • Dimerization
  • DNA
  • DNA - metabolism
  • DNA binding proteins
  • DNA-Binding Proteins - chemistry
  • DNA-Binding Proteins - genetics
  • DNA-Binding Proteins - metabolism
  • Fluorescence Polarization
  • Gene expression
  • Genetic transcription
  • Life Sciences
  • Magnetic Resonance Spectroscopy
  • Models
  • Models, Molecular
  • Molecular
  • Molecular Biology
  • Molecular Sequence Data
  • Mutation
  • Peptide Fragments
  • Peptide Fragments - chemistry
  • Physiological aspects
  • Protein Conformation
  • Protein Folding
  • Protein Structure
  • Protein Structure, Tertiary
  • Tertiary
ispartof: Nature structural & molecular biology, 2003-03, Vol.10 (3), p.212-218
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.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 1072-8368
fulltext: fulltext
issn:
  • 1072-8368
  • 1545-9993
  • 2331-365X
  • 1545-9985
url: Link


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descriptionH-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.
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subjectAmino Acid Sequence ; Bacterial Proteins ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Binding Proteins ; Biochemistry ; Biochemistry, Molecular Biology ; Conserved Sequence ; Dimerization ; DNA ; DNA - metabolism ; DNA binding proteins ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Fluorescence Polarization ; Gene expression ; Genetic transcription ; Life Sciences ; Magnetic Resonance Spectroscopy ; Models ; Models, Molecular ; Molecular ; Molecular Biology ; Molecular Sequence Data ; Mutation ; Peptide Fragments ; Peptide Fragments - chemistry ; Physiological aspects ; Protein Conformation ; Protein Folding ; Protein Structure ; Protein Structure, Tertiary ; Tertiary
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descriptionH-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.
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3Bacterial Proteins - genetics
4Bacterial Proteins - metabolism
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9Dimerization
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17Gene expression
18Genetic transcription
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20Magnetic Resonance Spectroscopy
21Models
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23Molecular
24Molecular Biology
25Molecular Sequence Data
26Mutation
27Peptide Fragments
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29Physiological aspects
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abstractH-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.
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pmid12592399
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