Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.
Identifieur interne : 001075 ( PubMed/Checkpoint ); précédent : 001074; suivant : 001076Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.
Auteurs : Chung-Ke Chang [République populaire de Chine] ; Chia-Min Michael Chen ; Ming-Hui Chiang ; Yen-Lan Hsu ; Tai-Huang HuangSource :
- PloS one [ 1932-6203 ] ; 2013.
Descripteurs français
- KwdFr :
- Assemblage viral, Association médicamenteuse, Carbonate de calcium, Citrates, Cystine (), Maturation post-traductionnelle des protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Mutagenèse dirigée, Oxyde de magnésium, Phosphorylation, Protéines nucléocapside (), Protéines nucléocapside (génétique), Substitution d'acide aminé, Virus du SRAS.
- MESH :
- génétique : Protéines nucléocapside.
- Assemblage viral, Association médicamenteuse, Carbonate de calcium, Citrates, Cystine, Maturation post-traductionnelle des protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Mutagenèse dirigée, Oxyde de magnésium, Phosphorylation, Protéines nucléocapside, Substitution d'acide aminé, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Substitution, Calcium Carbonate, Citrates, Cystine (chemistry), Drug Combinations, Magnesium Oxide, Models, Molecular, Mutagenesis, Site-Directed, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Phosphorylation, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Processing, Post-Translational, SARS Virus, Virus Assembly.
- MESH :
- chemical , chemistry : Cystine, Nucleocapsid Proteins.
- chemical , genetics : Nucleocapsid Proteins.
- chemical : Calcium Carbonate, Citrates, Drug Combinations, Magnesium Oxide.
- Amino Acid Substitution, Models, Molecular, Mutagenesis, Site-Directed, Phosphorylation, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Processing, Post-Translational, SARS Virus, Virus Assembly.
Abstract
The nucleocapsid (N) phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genome into a helical ribonucleocapsid and plays a fundamental role during viral self-assembly. The N protein consists of two structural domains interspersed between intrinsically disordered regions and dimerizes through the C-terminal structural domain (CTD). A key activity of the protein is the ability to oligomerize during capsid formation by utilizing the dimer as a building block, but the structural and mechanistic bases of this activity are not well understood. By disulfide trapping technique we measured the amount of transient oligomers of N protein mutants with strategically located cysteine residues and showed that CTD acts as a primary transient oligomerization domain in solution. The data is consistent with the helical oligomer packing model of N protein observed in crystal. A systematic study of the oligomerization behavior revealed that altering the intermolecular electrostatic repulsion through changes in solution salt concentration or phosphorylation-mimicking mutations affects oligomerization propensity. We propose a biophysical mechanism where electrostatic repulsion acts as a switch to regulate N protein oligomerization.
DOI: 10.1371/journal.pone.0065045
PubMed: 23717688
Affiliations:
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pubmed:23717688Le document en format XML
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<front><div type="abstract" xml:lang="en">The nucleocapsid (N) phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genome into a helical ribonucleocapsid and plays a fundamental role during viral self-assembly. The N protein consists of two structural domains interspersed between intrinsically disordered regions and dimerizes through the C-terminal structural domain (CTD). A key activity of the protein is the ability to oligomerize during capsid formation by utilizing the dimer as a building block, but the structural and mechanistic bases of this activity are not well understood. By disulfide trapping technique we measured the amount of transient oligomers of N protein mutants with strategically located cysteine residues and showed that CTD acts as a primary transient oligomerization domain in solution. The data is consistent with the helical oligomer packing model of N protein observed in crystal. A systematic study of the oligomerization behavior revealed that altering the intermolecular electrostatic repulsion through changes in solution salt concentration or phosphorylation-mimicking mutations affects oligomerization propensity. We propose a biophysical mechanism where electrostatic repulsion acts as a switch to regulate N protein oligomerization.</div>
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<Reference><Citation>J Virol. 2009 Oct;83(20):10616-26</Citation>
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<affiliations><list><country><li>République populaire de Chine</li>
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<tree><noCountry><name sortKey="Chen, Chia Min Michael" sort="Chen, Chia Min Michael" uniqKey="Chen C" first="Chia-Min Michael" last="Chen">Chia-Min Michael Chen</name>
<name sortKey="Chiang, Ming Hui" sort="Chiang, Ming Hui" uniqKey="Chiang M" first="Ming-Hui" last="Chiang">Ming-Hui Chiang</name>
<name sortKey="Hsu, Yen Lan" sort="Hsu, Yen Lan" uniqKey="Hsu Y" first="Yen-Lan" last="Hsu">Yen-Lan Hsu</name>
<name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name>
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<country name="République populaire de Chine"><noRegion><name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name>
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