Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: self-association analysis and nucleic acid binding characterization.
Identifieur interne : 003F61 ( Main/Exploration ); précédent : 003F60; suivant : 003F62Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: self-association analysis and nucleic acid binding characterization.
Auteurs : Haibin Luo [République populaire de Chine] ; Jing Chen ; Kaixian Chen ; Xu Shen ; Hualiang JiangSource :
- Biochemistry [ 0006-2960 ] ; 2006.
Descripteurs français
- KwdFr :
- ARN viral (), ARN viral (génétique), ARN viral (métabolisme), Assemblage viral (physiologie), Chromatographie sur gel, Dimérisation, Délétion de séquence, Génome viral (physiologie), Liaison aux protéines (génétique), Nucléocapside (), Nucléocapside (génétique), Nucléocapside (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Sites de fixation (génétique), Structure tertiaire des protéines (génétique), Séquence d'acides aminés (génétique), Virus du SRAS (), Virus du SRAS (physiologie), Électricité statique.
- MESH :
- génétique : ARN viral, Liaison aux protéines, Nucléocapside, Protéines nucléocapside, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés.
- métabolisme : ARN viral, Nucléocapside, Protéines nucléocapside.
- physiologie : Assemblage viral, Génome viral, Virus du SRAS.
- ARN viral, Chromatographie sur gel, Dimérisation, Délétion de séquence, Nucléocapside, Protéines nucléocapside, Virus du SRAS, Électricité statique.
English descriptors
- KwdEn :
- Amino Acid Sequence (genetics), Binding Sites (genetics), Chromatography, Gel, Dimerization, Genome, Viral (physiology), Nucleocapsid (chemistry), Nucleocapsid (genetics), Nucleocapsid (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Binding (genetics), Protein Structure, Tertiary (genetics), RNA, Viral (chemistry), RNA, Viral (genetics), RNA, Viral (metabolism), SARS Virus (chemistry), SARS Virus (physiology), Sequence Deletion, Static Electricity, Virus Assembly (physiology).
- MESH :
- chemical , chemistry : Nucleocapsid Proteins, RNA, Viral.
- chemistry : Nucleocapsid, SARS Virus.
- genetics : Amino Acid Sequence, Binding Sites, Nucleocapsid, Nucleocapsid Proteins, Protein Binding, Protein Structure, Tertiary, RNA, Viral.
- metabolism : Nucleocapsid, Nucleocapsid Proteins, RNA, Viral.
- physiology : Genome, Viral, SARS Virus, Virus Assembly.
- Chromatography, Gel, Dimerization, Sequence Deletion, Static Electricity.
Abstract
Coronavirus nucleocapsid (N) protein envelops the genomic RNA to form long helical nucleocapsid during virion assembly. Since N protein oligomerization is usually a crucial step in this process, characterization of such an oligomerization will help in the understanding of the possible mechanisms for nucleocapsid formation. The N protein of severe acute respiratory syndrome coronavirus (SARS-CoV) was recently discovered to self-associate by its carboxyl terminus. In this study, to further address the detailed understanding of the association feature of this C-terminus, its oligomerization was systematically investigated by size exclusion chromatography and chemical cross-linking assays. Our results clearly indicated that the C-terminal domain of SARS-CoV N protein could form not only dimers but also trimers, tetramers, and hexamers. Further analyses against six deletion mutants showed that residues 343-402 were necessary and sufficient for this C-terminus oligomerization. Although this segment contains many charged residues, differences in ionic strength have no effects on its oligomerization, indicating the absence of electrostatic force in SARS-CoV N protein C-terminus self-association. Gel shift assay results revealed that the SARS-CoV N protein C-terminus is also able to associate with nucleic acids and residues 363-382 are the responsible interaction partner, demonstrating that this fragment might involve genomic RNA binding sites. The fact that nucleic acid binding could promote the SARS-CoV N protein C-terminus to form high-order oligomers implies that the oligomeric SARS-CoV N protein probably combines with the viral genomic RNA in triggering long nucleocapsid formation.
DOI: 10.1021/bi0609319
PubMed: 17002283
Affiliations:
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Le document en format XML
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Chen</name></author><author><name sortKey="Chen, Kaixian" sort="Chen, Kaixian" uniqKey="Chen K" first="Kaixian" last="Chen">Kaixian Chen</name></author><author><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name></author><author><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:17002283</idno><idno type="pmid">17002283</idno><idno type="doi">10.1021/bi0609319</idno><idno type="wicri:Area/PubMed/Corpus">002078</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002078</idno><idno type="wicri:Area/PubMed/Curation">002078</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002078</idno><idno type="wicri:Area/PubMed/Checkpoint">002269</idno><idno type="wicri:explorRef" 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China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203</wicri:regionArea><wicri:noRegion>Shanghai 201203</wicri:noRegion></affiliation></author><author><name sortKey="Chen, Jing" sort="Chen, Jing" uniqKey="Chen J" first="Jing" last="Chen">Jing Chen</name></author><author><name sortKey="Chen, Kaixian" sort="Chen, Kaixian" uniqKey="Chen K" first="Kaixian" last="Chen">Kaixian Chen</name></author><author><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name></author><author><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (genetics)</term><term>Binding Sites (genetics)</term><term>Chromatography, Gel</term><term>Dimerization</term><term>Genome, Viral (physiology)</term><term>Nucleocapsid (chemistry)</term><term>Nucleocapsid (genetics)</term><term>Nucleocapsid (metabolism)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Binding (genetics)</term><term>Protein Structure, Tertiary (genetics)</term><term>RNA, Viral (chemistry)</term><term>RNA, Viral (genetics)</term><term>RNA, Viral (metabolism)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (physiology)</term><term>Sequence Deletion</term><term>Static Electricity</term><term>Virus Assembly (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral ()</term><term>ARN viral (génétique)</term><term>ARN viral (métabolisme)</term><term>Assemblage viral (physiologie)</term><term>Chromatographie sur gel</term><term>Dimérisation</term><term>Délétion de séquence</term><term>Génome viral (physiologie)</term><term>Liaison aux protéines (génétique)</term><term>Nucléocapside ()</term><term>Nucléocapside (génétique)</term><term>Nucléocapside (métabolisme)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (génétique)</term><term>Protéines nucléocapside (métabolisme)</term><term>Sites de fixation (génétique)</term><term>Structure tertiaire des protéines (génétique)</term><term>Séquence d'acides aminés (génétique)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (physiologie)</term><term>Électricité statique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Nucleocapsid</term><term>Nucleocapsid Proteins</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN viral</term><term>Liaison aux protéines</term><term>Nucléocapside</term><term>Protéines nucléocapside</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid</term><term>Nucleocapsid Proteins</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term><term>Nucléocapside</term><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Assemblage viral</term><term>Génome viral</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Genome, Viral</term><term>SARS Virus</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term><term>Dimerization</term><term>Sequence Deletion</term><term>Static Electricity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ARN viral</term><term>Chromatographie sur gel</term><term>Dimérisation</term><term>Délétion de séquence</term><term>Nucléocapside</term><term>Protéines nucléocapside</term><term>Virus du SRAS</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronavirus nucleocapsid (N) protein envelops the genomic RNA to form long helical nucleocapsid during virion assembly. Since N protein oligomerization is usually a crucial step in this process, characterization of such an oligomerization will help in the understanding of the possible mechanisms for nucleocapsid formation. The N protein of severe acute respiratory syndrome coronavirus (SARS-CoV) was recently discovered to self-associate by its carboxyl terminus. In this study, to further address the detailed understanding of the association feature of this C-terminus, its oligomerization was systematically investigated by size exclusion chromatography and chemical cross-linking assays. Our results clearly indicated that the C-terminal domain of SARS-CoV N protein could form not only dimers but also trimers, tetramers, and hexamers. Further analyses against six deletion mutants showed that residues 343-402 were necessary and sufficient for this C-terminus oligomerization. Although this segment contains many charged residues, differences in ionic strength have no effects on its oligomerization, indicating the absence of electrostatic force in SARS-CoV N protein C-terminus self-association. Gel shift assay results revealed that the SARS-CoV N protein C-terminus is also able to associate with nucleic acids and residues 363-382 are the responsible interaction partner, demonstrating that this fragment might involve genomic RNA binding sites. The fact that nucleic acid binding could promote the SARS-CoV N protein C-terminus to form high-order oligomers implies that the oligomeric SARS-CoV N protein probably combines with the viral genomic RNA in triggering long nucleocapsid formation.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Chen, Jing" sort="Chen, Jing" uniqKey="Chen J" first="Jing" last="Chen">Jing Chen</name><name sortKey="Chen, Kaixian" sort="Chen, Kaixian" uniqKey="Chen K" first="Kaixian" last="Chen">Kaixian Chen</name><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Luo, Haibin" sort="Luo, Haibin" uniqKey="Luo H" first="Haibin" last="Luo">Haibin Luo</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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