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Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging.

Identifieur interne : 001A20 ( PubMed/Curation ); précédent : 001A19; suivant : 001A21

Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging.

Auteurs : Chung-Ke Chang [République populaire de Chine] ; Yen-Lan Hsu ; Yuan-Hsiang Chang ; Fa-An Chao ; Ming-Chya Wu ; Yu-Shan Huang ; Chin-Kun Hu ; Tai-Huang Huang

Source :

Journal of virology [ 1098-5514 ] ; 2009.

RBID : pubmed:19052082

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Binding Sites, Electrophoretic Mobility Shift Assay, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Protein Binding, Protein Structure, Secondary, RNA, Viral (metabolism), Ribonucleoproteins (chemistry), Ribonucleoproteins (genetics), SARS Virus (chemistry), SARS Virus (genetics), Scattering, Small Angle, Sequence Alignment, X-Ray Diffraction.
MESH :
- chemical , chemistry : Nucleocapsid Proteins, Ribonucleoproteins.
- chemical , genetics : Nucleocapsid Proteins, Ribonucleoproteins.
- chemical , metabolism : RNA, Viral.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- Amino Acid Sequence, Binding Sites, Electrophoretic Mobility Shift Assay, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Scattering, Small Angle, Sequence Alignment, X-Ray Diffraction.

Abstract

The nucleocapsid protein (N) of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genomic RNA and is crucial for viability. However, the RNA-binding mechanism is poorly understood. We have shown previously that the N protein contains two structural domains--the N-terminal domain (NTD; residues 45 to 181) and the C-terminal dimerization domain (CTD; residues 248 to 365)--flanked by long stretches of disordered regions accounting for almost half of the entire sequence. Small-angle X-ray scattering data show that the protein is in an extended conformation and that the two structural domains of the SARS-CoV N protein are far apart. Both the NTD and the CTD have been shown to bind RNA. Here we show that all disordered regions are also capable of binding to RNA. Constructs containing multiple RNA-binding regions showed Hill coefficients greater than 1, suggesting that the N protein binds to RNA cooperatively. The effect can be explained by the "coupled-allostery" model, devised to explain the allosteric effect in a multidomain regulatory system. Although the N proteins of different coronaviruses share very low sequence homology, the physicochemical features described above may be conserved across different groups of Coronaviridae. The current results underscore the important roles of multisite nucleic acid binding and intrinsic disorder in N protein function and RNP packaging.

DOI: 10.1128/JVI.02001-08
PubMed: 19052082

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Le document en format XML

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<term>Molecular Sequence Data</term>
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<term>Données de séquences moléculaires</term>
<term>Liaison aux protéines</term>
<term>Protéines nucléocapside ()</term>
<term>Protéines nucléocapside (génétique)</term>
<term>Ribonucléoprotéines ()</term>
<term>Ribonucléoprotéines (génétique)</term>
<term>Sites de fixation</term>
<term>Spectroscopie par résonance magnétique</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Test de retard de migration électrophorétique</term>
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<term>Virus du SRAS (génétique)</term>
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<front><div type="abstract" xml:lang="en">The nucleocapsid protein (N) of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genomic RNA and is crucial for viability. However, the RNA-binding mechanism is poorly understood. We have shown previously that the N protein contains two structural domains--the N-terminal domain (NTD; residues 45 to 181) and the C-terminal dimerization domain (CTD; residues 248 to 365)--flanked by long stretches of disordered regions accounting for almost half of the entire sequence. Small-angle X-ray scattering data show that the protein is in an extended conformation and that the two structural domains of the SARS-CoV N protein are far apart. Both the NTD and the CTD have been shown to bind RNA. Here we show that all disordered regions are also capable of binding to RNA. Constructs containing multiple RNA-binding regions showed Hill coefficients greater than 1, suggesting that the N protein binds to RNA cooperatively. The effect can be explained by the "coupled-allostery" model, devised to explain the allosteric effect in a multidomain regulatory system. Although the N proteins of different coronaviruses share very low sequence homology, the physicochemical features described above may be conserved across different groups of Coronaviridae. The current results underscore the important roles of multisite nucleic acid binding and intrinsic disorder in N protein function and RNP packaging.</div>
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Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging.

Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging.

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