The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.
Identifieur interne : 001B70 ( Ncbi/Curation ); précédent : 001B69; suivant : 001B71The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.
Auteurs : Yingchun Zeng [République populaire de Chine] ; Linbai Ye ; Shengli Zhu ; Hong Zheng ; Peng Zhao ; Weijia Cai ; Liya Su ; Yinglong She ; Zhenghui WuSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2008.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Nuclear Proteins, Nucleocapsid Proteins.
- chemical , metabolism : Nuclear Proteins, Nucleocapsid Proteins.
- chemistry : SARS Virus.
- metabolism : SARS Virus.
- Binding Sites, HeLa Cells, Humans, Phosphorylation, Protein Binding.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid (N) protein of SARS-CoV encapsidates the viral RNA and plays an important role in virus particle assembly and release. In this study, the N protein of SARS-CoV was found to associate with B23, a phosphoprotein in nucleolus, in vitro and in vivo. Mapping studies localized the critical N sequences for this interaction to amino acid residues 175-210, which included a serine/arginine (SR)-rich domain. In vitro phosphorylation assay showed that the N protein inhibited the B23 phosphorylation at Thr199.
DOI: 10.1016/j.bbrc.2008.01.096
PubMed: 18243139
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pubmed:18243139Le document en format XML
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<author><name sortKey="Cai, Weijia" sort="Cai, Weijia" uniqKey="Cai W" first="Weijia" last="Cai">Weijia Cai</name>
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<author><name sortKey="Zheng, Hong" sort="Zheng, Hong" uniqKey="Zheng H" first="Hong" last="Zheng">Hong Zheng</name>
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<author><name sortKey="Zhao, Peng" sort="Zhao, Peng" uniqKey="Zhao P" first="Peng" last="Zhao">Peng Zhao</name>
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<author><name sortKey="Cai, Weijia" sort="Cai, Weijia" uniqKey="Cai W" first="Weijia" last="Cai">Weijia Cai</name>
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<author><name sortKey="She, Yinglong" sort="She, Yinglong" uniqKey="She Y" first="Yinglong" last="She">Yinglong She</name>
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<author><name sortKey="Wu, Zhenghui" sort="Wu, Zhenghui" uniqKey="Wu Z" first="Zhenghui" last="Wu">Zhenghui Wu</name>
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<series><title level="j">Biochemical and biophysical research communications</title>
<idno type="eISSN">1090-2104</idno>
<imprint><date when="2008" type="published">2008</date>
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<term>HeLa Cells</term>
<term>Humans</term>
<term>Nuclear Proteins (chemistry)</term>
<term>Nuclear Proteins (metabolism)</term>
<term>Nucleocapsid Proteins (chemistry)</term>
<term>Nucleocapsid Proteins (metabolism)</term>
<term>Phosphorylation</term>
<term>Protein Binding</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HeLa</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Phosphorylation</term>
<term>Protéines nucléaires ()</term>
<term>Protéines nucléaires (métabolisme)</term>
<term>Protéines nucléocapside ()</term>
<term>Protéines nucléocapside (métabolisme)</term>
<term>Sites de fixation</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nuclear Proteins</term>
<term>Nucleocapsid Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nuclear Proteins</term>
<term>Nucleocapsid Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines nucléaires</term>
<term>Protéines nucléocapside</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Phosphorylation</term>
<term>Protein Binding</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Phosphorylation</term>
<term>Protéines nucléaires</term>
<term>Protéines nucléocapside</term>
<term>Sites de fixation</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid (N) protein of SARS-CoV encapsidates the viral RNA and plays an important role in virus particle assembly and release. In this study, the N protein of SARS-CoV was found to associate with B23, a phosphoprotein in nucleolus, in vitro and in vivo. Mapping studies localized the critical N sequences for this interaction to amino acid residues 175-210, which included a serine/arginine (SR)-rich domain. In vitro phosphorylation assay showed that the N protein inhibited the B23 phosphorylation at Thr199.</div>
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