Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.
Identifieur interne : 004680 ( Main/Exploration ); précédent : 004679; suivant : 004681Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.
Auteurs : I-Mei Yu [États-Unis] ; Christin L T. Gustafson ; Jianbo Diao ; John W. Burgner ; Zhihong Li ; Jingqiang Zhang ; Jue ChenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2005.
Descripteurs français
- KwdFr :
- ADN simple brin (), ARN (), Acides nucléiques (métabolisme), Chromatographie, Coloration à l'argent, Diffusion de rayonnements, Dimérisation, Escherichia coli (métabolisme), Liaison aux protéines, Lumière, Mutagenèse, Mutation, Plasmides (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Protéines recombinantes (), Réactifs réticulants (pharmacologie), Structure tertiaire des protéines, Ultracentrifugation, Virus du SRAS (métabolisme), Électrophorèse sur gel de polyacrylamide.
- MESH :
- métabolisme : Acides nucléiques, Escherichia coli, Plasmides, Protéines nucléocapside, Virus du SRAS.
- pharmacologie : Réactifs réticulants.
- ADN simple brin, ARN, Chromatographie, Coloration à l'argent, Diffusion de rayonnements, Dimérisation, Liaison aux protéines, Lumière, Mutagenèse, Mutation, Protéines nucléocapside, Protéines recombinantes, Structure tertiaire des protéines, Ultracentrifugation, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Chromatography, Cross-Linking Reagents (pharmacology), DNA, Single-Stranded (chemistry), Dimerization, Electrophoresis, Polyacrylamide Gel, Escherichia coli (metabolism), Light, Mutagenesis, Mutation, Nucleic Acids (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Plasmids (metabolism), Protein Binding, Protein Structure, Tertiary, RNA (chemistry), Recombinant Proteins (chemistry), SARS Virus (metabolism), Scattering, Radiation, Silver Staining, Ultracentrifugation.
- MESH :
- chemical , chemistry : DNA, Single-Stranded, Nucleocapsid Proteins, RNA, Recombinant Proteins.
- chemical , metabolism : Nucleic Acids, Nucleocapsid Proteins.
- chemical , pharmacology : Cross-Linking Reagents.
- metabolism : Escherichia coli, Plasmids, SARS Virus.
- Chromatography, Dimerization, Electrophoresis, Polyacrylamide Gel, Light, Mutagenesis, Mutation, Protein Binding, Protein Structure, Tertiary, Scattering, Radiation, Silver Staining, Ultracentrifugation.
Abstract
The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The viral nucleocapsid (N) protein plays an essential role in viral RNA packaging. In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking. Dimeric N proteins self-associate into tetramers and higher molecular weight oligomers at high concentrations. The dimerization domain of N was mapped through studies of the oligomeric states of several truncated mutants. Although mutants consisting of residues 1-210 and 1-284 fold as monomers, constructs consisting of residues 211-422 and 285-422 efficiently form dimers. When in excess, the truncated construct 285-422 inhibits the homodimerization of full-length N protein by forming a heterodimer with the full-length N protein. These results suggest that the N protein oligomerization involves the C-terminal residues 285-422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly.
DOI: 10.1074/jbc.M501015200
PubMed: 15849181
Affiliations:
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Le document en format XML
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<term>Cross-Linking Reagents (pharmacology)</term>
<term>DNA, Single-Stranded (chemistry)</term>
<term>Dimerization</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Escherichia coli (metabolism)</term>
<term>Light</term>
<term>Mutagenesis</term>
<term>Mutation</term>
<term>Nucleic Acids (metabolism)</term>
<term>Nucleocapsid Proteins (chemistry)</term>
<term>Nucleocapsid Proteins (metabolism)</term>
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<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
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<term>Recombinant Proteins (chemistry)</term>
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<term>Silver Staining</term>
<term>Ultracentrifugation</term>
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<term>ARN ()</term>
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<term>Chromatographie</term>
<term>Coloration à l'argent</term>
<term>Diffusion de rayonnements</term>
<term>Dimérisation</term>
<term>Escherichia coli (métabolisme)</term>
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<term>Lumière</term>
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<term>Mutation</term>
<term>Plasmides (métabolisme)</term>
<term>Protéines nucléocapside ()</term>
<term>Protéines nucléocapside (métabolisme)</term>
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<term>Réactifs réticulants (pharmacologie)</term>
<term>Structure tertiaire des protéines</term>
<term>Ultracentrifugation</term>
<term>Virus du SRAS (métabolisme)</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<term>RNA</term>
<term>Recombinant Proteins</term>
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<term>SARS Virus</term>
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<term>Protéines nucléocapside</term>
<term>Virus du SRAS</term>
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<term>Dimerization</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Light</term>
<term>Mutagenesis</term>
<term>Mutation</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>Scattering, Radiation</term>
<term>Silver Staining</term>
<term>Ultracentrifugation</term>
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<term>Diffusion de rayonnements</term>
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<term>Lumière</term>
<term>Mutagenèse</term>
<term>Mutation</term>
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<front><div type="abstract" xml:lang="en">The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The viral nucleocapsid (N) protein plays an essential role in viral RNA packaging. In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking. Dimeric N proteins self-associate into tetramers and higher molecular weight oligomers at high concentrations. The dimerization domain of N was mapped through studies of the oligomeric states of several truncated mutants. Although mutants consisting of residues 1-210 and 1-284 fold as monomers, constructs consisting of residues 211-422 and 285-422 efficiently form dimers. When in excess, the truncated construct 285-422 inhibits the homodimerization of full-length N protein by forming a heterodimer with the full-length N protein. These results suggest that the N protein oligomerization involves the C-terminal residues 285-422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly.</div>
</front>
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<name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name>
<name sortKey="Diao, Jianbo" sort="Diao, Jianbo" uniqKey="Diao J" first="Jianbo" last="Diao">Jianbo Diao</name>
<name sortKey="Gustafson, Christin L T" sort="Gustafson, Christin L T" uniqKey="Gustafson C" first="Christin L T" last="Gustafson">Christin L T. Gustafson</name>
<name sortKey="Li, Zhihong" sort="Li, Zhihong" uniqKey="Li Z" first="Zhihong" last="Li">Zhihong Li</name>
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