SrasV1, Ncbi, Checkpoint, bibRecord, 002682

Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.

Identifieur interne : 002682 ( Ncbi/Checkpoint ); précédent : 002681; suivant : 002683

Transient 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 Huang

Source :

PloS one [ 1932-6203 ] ; 2013.

RBID : pubmed:23717688

Descripteurs français

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:

République populaire de Chine

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pubmed:23717688

Le document en format XML

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<term>Drug Combinations</term>
<term>Magnesium Oxide</term>
<term>Models, Molecular</term>
<term>Mutagenesis, Site-Directed</term>
<term>Nucleocapsid Proteins (chemistry)</term>
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<term>Association médicamenteuse</term>
<term>Carbonate de calcium</term>
<term>Citrates</term>
<term>Cystine ()</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Modèles moléculaires</term>
<term>Motifs et domaines d'intéraction protéique</term>
<term>Multimérisation de protéines</term>
<term>Mutagenèse dirigée</term>
<term>Oxyde de magnésium</term>
<term>Phosphorylation</term>
<term>Protéines nucléocapside ()</term>
<term>Protéines nucléocapside (génétique)</term>
<term>Substitution d'acide aminé</term>
<term>Virus du SRAS</term>
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<term>Protein Processing, Post-Translational</term>
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<term>Virus Assembly</term>
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<term>Association médicamenteuse</term>
<term>Carbonate de calcium</term>
<term>Citrates</term>
<term>Cystine</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Modèles moléculaires</term>
<term>Motifs et domaines d'intéraction protéique</term>
<term>Multimérisation de protéines</term>
<term>Mutagenèse dirigée</term>
<term>Oxyde de magnésium</term>
<term>Phosphorylation</term>
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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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Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.

Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki