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Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.

Identifieur interne : 004680 ( Main/Exploration ); précédent : 004679; suivant : 004681

Recombinant 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 Chen

Source :

RBID : pubmed:15849181

Descripteurs français

English descriptors

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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Le document en format XML

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<term>Dimerization</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Escherichia coli (metabolism)</term>
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<term>Mutagenesis</term>
<term>Mutation</term>
<term>Nucleic Acids (metabolism)</term>
<term>Nucleocapsid Proteins (chemistry)</term>
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<term>Lumière</term>
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<term>Protéines nucléocapside ()</term>
<term>Protéines nucléocapside (métabolisme)</term>
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<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>
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