SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.
Identifieur interne : 002461 ( Main/Exploration ); précédent : 002460; suivant : 002462SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.
Auteurs : Margaret A. Johnson [États-Unis] ; Amarnath Chatterjee ; Benjamin W. Neuman ; Kurt WüthrichSource :
- Journal of molecular biology [ 1089-8638 ] ; 2010.
Descripteurs français
- KwdFr :
- ARN viral (métabolisme), Conformation des protéines, Liaison aux protéines, Modèles moléculaires, Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (métabolisme), Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Structure tertiaire des protéines, Test de retard de migration électrophorétique, Virus du SRAS ().
- MESH :
- métabolisme : ARN viral, Protéines de liaison à l'ARN, Protéines virales non structurales.
- Conformation des protéines, Liaison aux protéines, Modèles moléculaires, Protéines de liaison à l'ARN, Protéines virales non structurales, Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Structure tertiaire des protéines, Test de retard de migration électrophorétique, Virus du SRAS.
English descriptors
- KwdEn :
- Electrophoretic Mobility Shift Assay, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, RNA, Viral (metabolism), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), SARS Virus (chemistry), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : RNA-Binding Proteins, Viral Nonstructural Proteins.
- chemical , metabolism : RNA, Viral, RNA-Binding Proteins, Viral Nonstructural Proteins.
- chemistry : SARS Virus.
- Electrophoretic Mobility Shift Assay, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary.
Abstract
Nonstructural protein 3 of the severe acute respiratory syndrome (SARS) coronavirus includes a "SARS-unique domain" (SUD) consisting of three globular domains separated by short linker peptide segments. This work reports NMR structure determinations of the C-terminal domain (SUD-C) and a two-domain construct (SUD-MC) containing the middle domain (SUD-M) and the C-terminal domain, and NMR data on the conformational states of the N-terminal domain (SUD-N) and the SUD-NM two-domain construct. Both SUD-N and SUD-NM are monomeric and globular in solution; in SUD-NM, there is high mobility in the two-residue interdomain linking sequence, with no preferred relative orientation of the two domains. SUD-C adopts a frataxin like fold and has structural similarity to DNA-binding domains of DNA-modifying enzymes. The structures of both SUD-M (previously determined) and SUD-C (from the present study) are maintained in SUD-MC, where the two domains are flexibly linked. Gel-shift experiments showed that both SUD-C and SUD-MC bind to single-stranded RNA and recognize purine bases more strongly than pyrimidine bases, whereby SUD-MC binds to a more restricted set of purine-containing RNA sequences than SUD-M. NMR chemical shift perturbation experiments with observations of (15)N-labeled proteins further resulted in delineation of RNA binding sites (i.e., in SUD-M, a positively charged surface area with a pronounced cavity, and in SUD-C, several residues of an anti-parallel beta-sheet). Overall, the present data provide evidence for molecular mechanisms involving the concerted actions of SUD-M and SUD-C, which result in specific RNA binding that might be unique to the SUD and, thus, to the SARS coronavirus.
DOI: 10.1016/j.jmb.2010.05.027
PubMed: 20493876
Affiliations:
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Johnson</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Chatterjee, Amarnath" sort="Chatterjee, Amarnath" uniqKey="Chatterjee A" first="Amarnath" last="Chatterjee">Amarnath Chatterjee</name></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W" last="Neuman">Benjamin W. Neuman</name></author><author><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="eISSN">1089-8638</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electrophoretic Mobility Shift Assay</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>RNA, Viral (metabolism)</term><term>RNA-Binding Proteins (chemistry)</term><term>RNA-Binding Proteins (metabolism)</term><term>SARS Virus (chemistry)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (métabolisme)</term><term>Conformation des protéines</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Protéines de liaison à l'ARN ()</term><term>Protéines de liaison à l'ARN (métabolisme)</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (métabolisme)</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Test de retard de migration électrophorétique</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA-Binding Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA, Viral</term><term>RNA-Binding Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term><term>Protéines de liaison à l'ARN</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoretic Mobility Shift Assay</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Protéines de liaison à l'ARN</term><term>Protéines virales non structurales</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Test de retard de migration électrophorétique</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nonstructural protein 3 of the severe acute respiratory syndrome (SARS) coronavirus includes a "SARS-unique domain" (SUD) consisting of three globular domains separated by short linker peptide segments. This work reports NMR structure determinations of the C-terminal domain (SUD-C) and a two-domain construct (SUD-MC) containing the middle domain (SUD-M) and the C-terminal domain, and NMR data on the conformational states of the N-terminal domain (SUD-N) and the SUD-NM two-domain construct. Both SUD-N and SUD-NM are monomeric and globular in solution; in SUD-NM, there is high mobility in the two-residue interdomain linking sequence, with no preferred relative orientation of the two domains. SUD-C adopts a frataxin like fold and has structural similarity to DNA-binding domains of DNA-modifying enzymes. The structures of both SUD-M (previously determined) and SUD-C (from the present study) are maintained in SUD-MC, where the two domains are flexibly linked. Gel-shift experiments showed that both SUD-C and SUD-MC bind to single-stranded RNA and recognize purine bases more strongly than pyrimidine bases, whereby SUD-MC binds to a more restricted set of purine-containing RNA sequences than SUD-M. NMR chemical shift perturbation experiments with observations of (15)N-labeled proteins further resulted in delineation of RNA binding sites (i.e., in SUD-M, a positively charged surface area with a pronounced cavity, and in SUD-C, several residues of an anti-parallel beta-sheet). Overall, the present data provide evidence for molecular mechanisms involving the concerted actions of SUD-M and SUD-C, which result in specific RNA binding that might be unique to the SUD and, thus, to the SARS coronavirus.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Chatterjee, Amarnath" sort="Chatterjee, Amarnath" uniqKey="Chatterjee A" first="Amarnath" last="Chatterjee">Amarnath Chatterjee</name><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W" last="Neuman">Benjamin W. Neuman</name><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. 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