Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.
Identifieur interne : 002771 ( PubMed/Curation ); précédent : 002770; suivant : 002772Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.
Auteurs : I-Mei Yu [États-Unis] ; Christin L T. Gustafson ; Jianbo Diao ; John W. Burgner ; Zhihong Li ; Jingqiang Zhang ; Jue ChenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2005.
Descripteurs français
- KwdFr :
- ADN simple brin (), ARN (), Acides nucléiques (métabolisme), Chromatographie, Coloration à l'argent, Diffusion de rayonnements, Dimérisation, Escherichia coli (métabolisme), Liaison aux protéines, Lumière, Mutagenèse, Mutation, Plasmides (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Protéines recombinantes (), Réactifs réticulants (pharmacologie), Structure tertiaire des protéines, Ultracentrifugation, Virus du SRAS (métabolisme), Électrophorèse sur gel de polyacrylamide.
- MESH :
- métabolisme : Acides nucléiques, Escherichia coli, Plasmides, Protéines nucléocapside, Virus du SRAS.
- pharmacologie : Réactifs réticulants.
- ADN simple brin, ARN, Chromatographie, Coloration à l'argent, Diffusion de rayonnements, Dimérisation, Liaison aux protéines, Lumière, Mutagenèse, Mutation, Protéines nucléocapside, Protéines recombinantes, Structure tertiaire des protéines, Ultracentrifugation, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Chromatography, Cross-Linking Reagents (pharmacology), DNA, Single-Stranded (chemistry), Dimerization, Electrophoresis, Polyacrylamide Gel, Escherichia coli (metabolism), Light, Mutagenesis, Mutation, Nucleic Acids (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Plasmids (metabolism), Protein Binding, Protein Structure, Tertiary, RNA (chemistry), Recombinant Proteins (chemistry), SARS Virus (metabolism), Scattering, Radiation, Silver Staining, Ultracentrifugation.
- MESH :
- chemical , chemistry : DNA, Single-Stranded, Nucleocapsid Proteins, RNA, Recombinant Proteins.
- chemical , metabolism : Nucleic Acids, Nucleocapsid Proteins.
- chemical , pharmacology : Cross-Linking Reagents.
- metabolism : Escherichia coli, Plasmids, SARS Virus.
- Chromatography, Dimerization, Electrophoresis, Polyacrylamide Gel, Light, Mutagenesis, Mutation, Protein Binding, Protein Structure, Tertiary, Scattering, Radiation, Silver Staining, Ultracentrifugation.
Abstract
The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The viral nucleocapsid (N) protein plays an essential role in viral RNA packaging. In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking. Dimeric N proteins self-associate into tetramers and higher molecular weight oligomers at high concentrations. The dimerization domain of N was mapped through studies of the oligomeric states of several truncated mutants. Although mutants consisting of residues 1-210 and 1-284 fold as monomers, constructs consisting of residues 211-422 and 285-422 efficiently form dimers. When in excess, the truncated construct 285-422 inhibits the homodimerization of full-length N protein by forming a heterodimer with the full-length N protein. These results suggest that the N protein oligomerization involves the C-terminal residues 285-422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly.
DOI: 10.1074/jbc.M501015200
PubMed: 15849181
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pubmed:15849181Le document en format XML
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Gustafson</name></author><author><name sortKey="Diao, Jianbo" sort="Diao, Jianbo" uniqKey="Diao J" first="Jianbo" last="Diao">Jianbo Diao</name></author><author><name sortKey="Burgner, John W" sort="Burgner, John W" uniqKey="Burgner J" first="John W" last="Burgner">John W. Burgner</name></author><author><name sortKey="Li, Zhihong" sort="Li, Zhihong" uniqKey="Li Z" first="Zhihong" last="Li">Zhihong Li</name></author><author><name sortKey="Zhang, Jingqiang" sort="Zhang, Jingqiang" uniqKey="Zhang J" first="Jingqiang" last="Zhang">Jingqiang Zhang</name></author><author><name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15849181</idno><idno type="pmid">15849181</idno><idno type="doi">10.1074/jbc.M501015200</idno><idno type="wicri:Area/PubMed/Corpus">002771</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002771</idno><idno type="wicri:Area/PubMed/Curation">002771</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002771</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.</title><author><name sortKey="Yu, I Mei" sort="Yu, I Mei" uniqKey="Yu I" first="I-Mei" last="Yu">I-Mei Yu</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907</wicri:regionArea></affiliation></author><author><name sortKey="Gustafson, Christin L T" sort="Gustafson, Christin L T" uniqKey="Gustafson C" first="Christin L T" last="Gustafson">Christin L T. Gustafson</name></author><author><name sortKey="Diao, Jianbo" sort="Diao, Jianbo" uniqKey="Diao J" first="Jianbo" last="Diao">Jianbo Diao</name></author><author><name sortKey="Burgner, John W" sort="Burgner, John W" uniqKey="Burgner J" first="John W" last="Burgner">John W. Burgner</name></author><author><name sortKey="Li, Zhihong" sort="Li, Zhihong" uniqKey="Li Z" first="Zhihong" last="Li">Zhihong Li</name></author><author><name sortKey="Zhang, Jingqiang" sort="Zhang, Jingqiang" uniqKey="Zhang J" first="Jingqiang" last="Zhang">Jingqiang Zhang</name></author><author><name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography</term><term>Cross-Linking Reagents (pharmacology)</term><term>DNA, Single-Stranded (chemistry)</term><term>Dimerization</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Escherichia coli (metabolism)</term><term>Light</term><term>Mutagenesis</term><term>Mutation</term><term>Nucleic Acids (metabolism)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Plasmids (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>RNA (chemistry)</term><term>Recombinant Proteins (chemistry)</term><term>SARS Virus (metabolism)</term><term>Scattering, Radiation</term><term>Silver Staining</term><term>Ultracentrifugation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN simple brin ()</term><term>ARN ()</term><term>Acides nucléiques (métabolisme)</term><term>Chromatographie</term><term>Coloration à l'argent</term><term>Diffusion de rayonnements</term><term>Dimérisation</term><term>Escherichia coli (métabolisme)</term><term>Liaison aux protéines</term><term>Lumière</term><term>Mutagenèse</term><term>Mutation</term><term>Plasmides (métabolisme)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (métabolisme)</term><term>Protéines recombinantes ()</term><term>Réactifs réticulants (pharmacologie)</term><term>Structure tertiaire des protéines</term><term>Ultracentrifugation</term><term>Virus du SRAS (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Single-Stranded</term><term>Nucleocapsid Proteins</term><term>RNA</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleic Acids</term><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cross-Linking Reagents</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Plasmids</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides nucléiques</term><term>Escherichia coli</term><term>Plasmides</term><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Réactifs réticulants</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography</term><term>Dimerization</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Light</term><term>Mutagenesis</term><term>Mutation</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Scattering, Radiation</term><term>Silver Staining</term><term>Ultracentrifugation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN simple brin</term><term>ARN</term><term>Chromatographie</term><term>Coloration à l'argent</term><term>Diffusion de rayonnements</term><term>Dimérisation</term><term>Liaison aux protéines</term><term>Lumière</term><term>Mutagenèse</term><term>Mutation</term><term>Protéines nucléocapside</term><term>Protéines recombinantes</term><term>Structure tertiaire des protéines</term><term>Ultracentrifugation</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The viral nucleocapsid (N) protein plays an essential role in viral RNA packaging. In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking. Dimeric N proteins self-associate into tetramers and higher molecular weight oligomers at high concentrations. The dimerization domain of N was mapped through studies of the oligomeric states of several truncated mutants. Although mutants consisting of residues 1-210 and 1-284 fold as monomers, constructs consisting of residues 211-422 and 285-422 efficiently form dimers. When in excess, the truncated construct 285-422 inhibits the homodimerization of full-length N protein by forming a heterodimer with the full-length N protein. These results suggest that the N protein oligomerization involves the C-terminal residues 285-422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15849181</PMID><DateCompleted><Year>2005</Year><Month>07</Month><Day>19</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>280</Volume><Issue>24</Issue><PubDate><Year>2005</Year><Month>Jun</Month><Day>17</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.</ArticleTitle><Pagination><MedlinePgn>23280-6</MedlinePgn></Pagination><Abstract><AbstractText>The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The viral nucleocapsid (N) protein plays an essential role in viral RNA packaging. In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking. Dimeric N proteins self-associate into tetramers and higher molecular weight oligomers at high concentrations. The dimerization domain of N was mapped through studies of the oligomeric states of several truncated mutants. Although mutants consisting of residues 1-210 and 1-284 fold as monomers, constructs consisting of residues 211-422 and 285-422 efficiently form dimers. When in excess, the truncated construct 285-422 inhibits the homodimerization of full-length N protein by forming a heterodimer with the full-length N protein. These results suggest that the N protein oligomerization involves the C-terminal residues 285-422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>I-Mei</ForeName><Initials>IM</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gustafson</LastName><ForeName>Christin L T</ForeName><Initials>CL</Initials></Author><Author ValidYN="Y"><LastName>Diao</LastName><ForeName>Jianbo</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Burgner</LastName><ForeName>John W</ForeName><Initials>JW</Initials><Suffix>2nd</Suffix></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Zhihong</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Jingqiang</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Jue</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>04</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003432">Cross-Linking Reagents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004277">DNA, Single-Stranded</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009696">Nucleic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002845" MajorTopicYN="N">Chromatography</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003432" MajorTopicYN="N">Cross-Linking Reagents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004277" MajorTopicYN="N">DNA, Single-Stranded</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008027" MajorTopicYN="N">Light</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016296" MajorTopicYN="N">Mutagenesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009696" MajorTopicYN="N">Nucleic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012542" MajorTopicYN="N">Scattering, Radiation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016622" MajorTopicYN="N">Silver Staining</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014461" MajorTopicYN="N">Ultracentrifugation</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>4</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>7</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>4</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15849181</ArticleId><ArticleId IdType="pii">M501015200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M501015200</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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