Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.
Identifieur interne : 002682 ( Ncbi/Curation ); précédent : 002681; suivant : 002683Transient 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
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001190
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :001190
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :001075
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :002682
Links to Exploration step
pubmed:23717688Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.</title>
<author><name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan</wicri:regionArea>
<wicri:noRegion>Taiwan</wicri:noRegion>
</affiliation>
</author>
<author><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>
</author>
<author><name sortKey="Chiang, Ming Hui" sort="Chiang, Ming Hui" uniqKey="Chiang M" first="Ming-Hui" last="Chiang">Ming-Hui Chiang</name>
</author>
<author><name sortKey="Hsu, Yen Lan" sort="Hsu, Yen Lan" uniqKey="Hsu Y" first="Yen-Lan" last="Hsu">Yen-Lan Hsu</name>
</author>
<author><name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2013">2013</date>
<idno type="RBID">pubmed:23717688</idno>
<idno type="pmid">23717688</idno>
<idno type="doi">10.1371/journal.pone.0065045</idno>
<idno type="wicri:Area/PubMed/Corpus">001190</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001190</idno>
<idno type="wicri:Area/PubMed/Curation">001190</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001190</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001075</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001075</idno>
<idno type="wicri:Area/Ncbi/Merge">002682</idno>
<idno type="wicri:Area/Ncbi/Curation">002682</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.</title>
<author><name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan</wicri:regionArea>
<wicri:noRegion>Taiwan</wicri:noRegion>
</affiliation>
</author>
<author><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>
</author>
<author><name sortKey="Chiang, Ming Hui" sort="Chiang, Ming Hui" uniqKey="Chiang M" first="Ming-Hui" last="Chiang">Ming-Hui Chiang</name>
</author>
<author><name sortKey="Hsu, Yen Lan" sort="Hsu, Yen Lan" uniqKey="Hsu Y" first="Yen-Lan" last="Hsu">Yen-Lan Hsu</name>
</author>
<author><name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name>
</author>
</analytic>
<series><title level="j">PloS one</title>
<idno type="eISSN">1932-6203</idno>
<imprint><date when="2013" type="published">2013</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term>
<term>Calcium Carbonate</term>
<term>Citrates</term>
<term>Cystine (chemistry)</term>
<term>Drug Combinations</term>
<term>Magnesium Oxide</term>
<term>Models, Molecular</term>
<term>Mutagenesis, Site-Directed</term>
<term>Nucleocapsid Proteins (chemistry)</term>
<term>Nucleocapsid Proteins (genetics)</term>
<term>Phosphorylation</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Multimerization</term>
<term>Protein Processing, Post-Translational</term>
<term>SARS Virus</term>
<term>Virus Assembly</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Assemblage viral</term>
<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>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cystine</term>
<term>Nucleocapsid Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nucleocapsid Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Calcium Carbonate</term>
<term>Citrates</term>
<term>Drug Combinations</term>
<term>Magnesium Oxide</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines nucléocapside</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term>
<term>Models, Molecular</term>
<term>Mutagenesis, Site-Directed</term>
<term>Phosphorylation</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Multimerization</term>
<term>Protein Processing, Post-Translational</term>
<term>SARS Virus</term>
<term>Virus Assembly</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Assemblage viral</term>
<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>Substitution d'acide aminé</term>
<term>Virus du SRAS</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002682 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd -nk 002682 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= Ncbi |étape= Curation |type= RBID |clé= pubmed:23717688 |texte= Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/RBID.i -Sk "pubmed:23717688" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |