SrasV1, PubMed, Checkpoint, bibRecord, 001075

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

Identifieur interne : 001075 ( PubMed/Checkpoint ); précédent : 001074; suivant : 001076

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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<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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<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>
</noCountry>
<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>
</noRegion>
</country>
</tree>
</affiliations>
</record>

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{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    PubMed
   |étape=   Checkpoint
   |type=    RBID
   |clé=     pubmed:23717688
   |texte=   Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.
}}

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       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

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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.

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