Variable oligomerization modes in coronavirus non-structural protein 9.
Identifieur interne : 002F77 ( Main/Exploration ); précédent : 002F76; suivant : 002F78Variable oligomerization modes in coronavirus non-structural protein 9.
Auteurs : Rajesh Ponnusamy [Allemagne] ; Ralf Moll ; Thomas Weimar ; Jeroen R. Mesters ; Rolf HilgenfeldSource :
- Journal of molecular biology [ 1089-8638 ] ; 2008.
Descripteurs français
- KwdFr :
- ADN (métabolisme), Acides nucléiques (métabolisme), Coronavirus (), Cristallographie aux rayons X, Cystéine (métabolisme), Dimérisation, Glutaraldéhyde (pharmacologie), Modèles moléculaires, Oxydoréduction (), Polymères, Protéines de liaison à l'ARN (), Protéines mutantes (), Protéines virales (), Protéines virales non structurales (), Protéines virales non structurales (métabolisme), Réactifs réticulants (pharmacologie), Résonance plasmonique de surface, Solutions, Structure quaternaire des protéines, Structure secondaire des protéines, Substitution d'acide aminé (), Test de retard de migration électrophorétique.
- MESH :
- métabolisme : ADN, Acides nucléiques, Cystéine, Protéines virales non structurales.
- pharmacologie : Glutaraldéhyde, Réactifs réticulants.
- Coronavirus, Cristallographie aux rayons X, Dimérisation, Modèles moléculaires, Oxydoréduction, Polymères, Protéines de liaison à l'ARN, Protéines mutantes, Protéines virales, Protéines virales non structurales, Résonance plasmonique de surface, Solutions, Structure quaternaire des protéines, Structure secondaire des protéines, Substitution d'acide aminé, Test de retard de migration électrophorétique.
English descriptors
- KwdEn :
- Amino Acid Substitution (drug effects), Coronavirus (chemistry), Cross-Linking Reagents (pharmacology), Crystallography, X-Ray, Cysteine (metabolism), DNA (metabolism), Dimerization, Electrophoretic Mobility Shift Assay, Glutaral (pharmacology), Models, Molecular, Mutant Proteins (chemistry), Nucleic Acids (metabolism), Oxidation-Reduction (drug effects), Polymers, Protein Structure, Quaternary, Protein Structure, Secondary, RNA-Binding Proteins (chemistry), Solutions, Surface Plasmon Resonance, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism), Viral Proteins (chemistry).
- MESH :
- chemical , chemistry : Mutant Proteins, RNA-Binding Proteins, Viral Nonstructural Proteins, Viral Proteins.
- chemical , metabolism : Cysteine, DNA, Nucleic Acids, Viral Nonstructural Proteins.
- chemical , pharmacology : Cross-Linking Reagents, Glutaral.
- chemistry : Coronavirus.
- drug effects : Amino Acid Substitution, Oxidation-Reduction.
- Crystallography, X-Ray, Dimerization, Electrophoretic Mobility Shift Assay, Models, Molecular, Polymers, Protein Structure, Quaternary, Protein Structure, Secondary, Solutions, Surface Plasmon Resonance.
Abstract
Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.
DOI: 10.1016/j.jmb.2008.07.071
PubMed: 18694760
Affiliations:
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Le document en format XML
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Mesters</name></author><author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18694760</idno><idno type="pmid">18694760</idno><idno type="doi">10.1016/j.jmb.2008.07.071</idno><idno type="wicri:Area/PubMed/Corpus">001A87</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001A87</idno><idno type="wicri:Area/PubMed/Curation">001A87</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001A87</idno><idno type="wicri:Area/PubMed/Checkpoint">001974</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001974</idno><idno type="wicri:Area/Ncbi/Merge">001D15</idno><idno type="wicri:Area/Ncbi/Curation">001D15</idno><idno type="wicri:Area/Ncbi/Checkpoint">001D15</idno><idno type="wicri:Area/Main/Merge">003041</idno><idno type="wicri:Area/Main/Curation">002F77</idno><idno type="wicri:Area/Main/Exploration">002F77</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Variable oligomerization modes in coronavirus non-structural protein 9.</title><author><name sortKey="Ponnusamy, Rajesh" sort="Ponnusamy, Rajesh" uniqKey="Ponnusamy R" first="Rajesh" last="Ponnusamy">Rajesh Ponnusamy</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck</wicri:regionArea><wicri:noRegion>23538 Lübeck</wicri:noRegion><wicri:noRegion>23538 Lübeck</wicri:noRegion><wicri:noRegion>23538 Lübeck</wicri:noRegion></affiliation></author><author><name sortKey="Moll, Ralf" sort="Moll, Ralf" uniqKey="Moll R" first="Ralf" last="Moll">Ralf Moll</name></author><author><name sortKey="Weimar, Thomas" sort="Weimar, Thomas" uniqKey="Weimar T" first="Thomas" last="Weimar">Thomas Weimar</name></author><author><name sortKey="Mesters, Jeroen R" sort="Mesters, Jeroen R" uniqKey="Mesters J" first="Jeroen R" last="Mesters">Jeroen R. Mesters</name></author><author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="eISSN">1089-8638</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution (drug effects)</term><term>Coronavirus (chemistry)</term><term>Cross-Linking Reagents (pharmacology)</term><term>Crystallography, X-Ray</term><term>Cysteine (metabolism)</term><term>DNA (metabolism)</term><term>Dimerization</term><term>Electrophoretic Mobility Shift Assay</term><term>Glutaral (pharmacology)</term><term>Models, Molecular</term><term>Mutant Proteins (chemistry)</term><term>Nucleic Acids (metabolism)</term><term>Oxidation-Reduction (drug effects)</term><term>Polymers</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>RNA-Binding Proteins (chemistry)</term><term>Solutions</term><term>Surface Plasmon Resonance</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (metabolism)</term><term>Viral Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN (métabolisme)</term><term>Acides nucléiques (métabolisme)</term><term>Coronavirus ()</term><term>Cristallographie aux rayons X</term><term>Cystéine (métabolisme)</term><term>Dimérisation</term><term>Glutaraldéhyde (pharmacologie)</term><term>Modèles moléculaires</term><term>Oxydoréduction ()</term><term>Polymères</term><term>Protéines de liaison à l'ARN ()</term><term>Protéines mutantes ()</term><term>Protéines virales ()</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (métabolisme)</term><term>Réactifs réticulants (pharmacologie)</term><term>Résonance plasmonique de surface</term><term>Solutions</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Substitution d'acide aminé ()</term><term>Test de retard de migration électrophorétique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Mutant Proteins</term><term>RNA-Binding Proteins</term><term>Viral Nonstructural Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>DNA</term><term>Nucleic Acids</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cross-Linking Reagents</term><term>Glutaral</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Amino Acid Substitution</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN</term><term>Acides nucléiques</term><term>Cystéine</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glutaraldéhyde</term><term>Réactifs réticulants</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Electrophoretic Mobility Shift Assay</term><term>Models, Molecular</term><term>Polymers</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Solutions</term><term>Surface Plasmon Resonance</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Coronavirus</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Polymères</term><term>Protéines de liaison à l'ARN</term><term>Protéines mutantes</term><term>Protéines virales</term><term>Protéines virales non structurales</term><term>Résonance plasmonique de surface</term><term>Solutions</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Substitution d'acide aminé</term><term>Test de retard de migration électrophorétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name><name sortKey="Mesters, Jeroen R" sort="Mesters, Jeroen R" uniqKey="Mesters J" first="Jeroen R" last="Mesters">Jeroen R. Mesters</name><name sortKey="Moll, Ralf" sort="Moll, Ralf" uniqKey="Moll R" first="Ralf" last="Moll">Ralf Moll</name><name sortKey="Weimar, Thomas" sort="Weimar, Thomas" uniqKey="Weimar T" first="Thomas" last="Weimar">Thomas Weimar</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Ponnusamy, Rajesh" sort="Ponnusamy, Rajesh" uniqKey="Ponnusamy R" first="Rajesh" last="Ponnusamy">Rajesh Ponnusamy</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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