SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization.
Identifieur interne : 004647 ( Main/Exploration ); précédent : 004646; suivant : 004648SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization.
Auteurs : Haibin Luo [République populaire de Chine] ; Fei Ye ; Kaixian Chen ; Xu Shen ; Hualiang JiangSource :
- Biochemistry [ 0006-2960 ] ; 2005.
Descripteurs français
- KwdFr :
- Cartographie d'interactions entre protéines, Chromatographie sur gel, Motifs d'acides aminés, Protéines nucléocapside (), Protéines nucléocapside (génétique), Protéines recombinantes (), Structure quaternaire des protéines, Structure tertiaire des protéines, Techniques de double hybride, Virus du SRAS (), Virus du SRAS (métabolisme).
- MESH :
- génétique : Protéines nucléocapside.
- métabolisme : Virus du SRAS.
- Cartographie d'interactions entre protéines, Chromatographie sur gel, Motifs d'acides aminés, Protéines nucléocapside, Protéines recombinantes, Structure quaternaire des protéines, Structure tertiaire des protéines, Techniques de double hybride, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Motifs, Chromatography, Gel, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Protein Interaction Mapping, Protein Structure, Quaternary, Protein Structure, Tertiary, Recombinant Proteins (chemistry), SARS Virus (chemistry), SARS Virus (metabolism), Two-Hybrid System Techniques.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins, Recombinant Proteins.
- chemical , genetics : Nucleocapsid Proteins.
- chemistry : SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Motifs, Chromatography, Gel, Protein Interaction Mapping, Protein Structure, Quaternary, Protein Structure, Tertiary, Two-Hybrid System Techniques.
Abstract
The nucleocapsid (N) protein of SARS coronavirus (SARS-CoV) is reported to function in encapsidating the viral genomic RNA into helical nucleocapsid, and its self-association is believed to be vital in coating the viral genomic RNA. Characterization of SARS-CoV N multimerization may thereby help us better understand the coronavirus assembly. In the current work, using the yeast two-hybrid technique, an unexpected interaction between residues 1-210 and 211-290 (central region) of the SARS-CoV N protein was detected, and SPR results further revealed that the SR-rich motif (amino acids 183-197) of SARS-CoV N protein is responsible for such an interaction. Chemical cross-linking and gel-filtration analyses indicated that the residues 283-422 of the SARS-CoV N protein have multimeric ability, although the full-length N protein is prone to exist predominantly as dimers. In addition, the multimeric ability of the C-terminal domain of SARS-CoV N protein could be weakened by the SR-rich motif interaction with the central region (amino acids 211-290). All of these data suggested that the SR-rich motif of the SARS-CoV N protein might play an import role in the transformation of the SARS-CoV N protein between the dimer and multimer during its binding to its central region for self-association or dissociation. This current paper will hopefully provide some new ideas in studying SARS-CoV N multimerization.
DOI: 10.1021/bi051122c
PubMed: 16285739
Affiliations:
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sortKey="Ye, Fei" sort="Ye, Fei" uniqKey="Ye F" first="Fei" last="Ye">Fei Ye</name></author><author><name sortKey="Chen, Kaixian" sort="Chen, Kaixian" uniqKey="Chen K" first="Kaixian" last="Chen">Kaixian Chen</name></author><author><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name></author><author><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16285739</idno><idno type="pmid">16285739</idno><idno type="doi">10.1021/bi051122c</idno><idno type="wicri:Area/PubMed/Corpus">002449</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002449</idno><idno type="wicri:Area/PubMed/Curation">002449</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002449</idno><idno 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Biological Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai 201203, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai 201203</wicri:regionArea><wicri:noRegion>Shanghai 201203</wicri:noRegion></affiliation></author><author><name sortKey="Ye, Fei" sort="Ye, Fei" uniqKey="Ye F" first="Fei" last="Ye">Fei Ye</name></author><author><name sortKey="Chen, Kaixian" sort="Chen, Kaixian" uniqKey="Chen K" first="Kaixian" last="Chen">Kaixian Chen</name></author><author><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name></author><author><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Chromatography, Gel</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (genetics)</term><term>Protein Interaction Mapping</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Recombinant Proteins (chemistry)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (metabolism)</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cartographie d'interactions entre protéines</term><term>Chromatographie sur gel</term><term>Motifs d'acides aminés</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (génétique)</term><term>Protéines recombinantes ()</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Techniques de double hybride</term><term>Virus du SRAS ()</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Chromatography, Gel</term><term>Protein Interaction Mapping</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cartographie d'interactions entre protéines</term><term>Chromatographie sur gel</term><term>Motifs d'acides aminés</term><term>Protéines nucléocapside</term><term>Protéines recombinantes</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Techniques de double hybride</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The nucleocapsid (N) protein of SARS coronavirus (SARS-CoV) is reported to function in encapsidating the viral genomic RNA into helical nucleocapsid, and its self-association is believed to be vital in coating the viral genomic RNA. Characterization of SARS-CoV N multimerization may thereby help us better understand the coronavirus assembly. In the current work, using the yeast two-hybrid technique, an unexpected interaction between residues 1-210 and 211-290 (central region) of the SARS-CoV N protein was detected, and SPR results further revealed that the SR-rich motif (amino acids 183-197) of SARS-CoV N protein is responsible for such an interaction. Chemical cross-linking and gel-filtration analyses indicated that the residues 283-422 of the SARS-CoV N protein have multimeric ability, although the full-length N protein is prone to exist predominantly as dimers. In addition, the multimeric ability of the C-terminal domain of SARS-CoV N protein could be weakened by the SR-rich motif interaction with the central region (amino acids 211-290). All of these data suggested that the SR-rich motif of the SARS-CoV N protein might play an import role in the transformation of the SARS-CoV N protein between the dimer and multimer during its binding to its central region for self-association or dissociation. This current paper will hopefully provide some new ideas in studying SARS-CoV N multimerization.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Chen, Kaixian" sort="Chen, Kaixian" uniqKey="Chen K" first="Kaixian" last="Chen">Kaixian Chen</name><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name><name sortKey="Ye, Fei" sort="Ye, Fei" uniqKey="Ye F" first="Fei" last="Ye">Fei Ye</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Luo, Haibin" sort="Luo, Haibin" uniqKey="Luo H" first="Haibin" last="Luo">Haibin Luo</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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