Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.
Identifieur interne : 002B28 ( Main/Exploration ); précédent : 002B27; suivant : 002B29Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.
Auteurs : Chun-Yu Huang [Taïwan] ; Yen-Lan Hsu ; Wan-Ling Chiang ; Ming-Hon HouSource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2009.
Descripteurs français
- KwdFr :
- Acides nucléiques (métabolisme), Coronavirus humain OC43 (), Dichroïsme circulaire, Glutaraldéhyde (), Humains, Multimérisation de protéines, Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Protéines recombinantes (), Protéines recombinantes (métabolisme), Sites de fixation, Spectrométrie de fluorescence, Stabilité protéique, Urée ().
- MESH :
- métabolisme : Acides nucléiques, Protéines de liaison à l'ARN, Protéines nucléocapside, Protéines recombinantes.
- Coronavirus humain OC43, Dichroïsme circulaire, Glutaraldéhyde, Humains, Multimérisation de protéines, Protéines de liaison à l'ARN, Protéines nucléocapside, Protéines recombinantes, Sites de fixation, Spectrométrie de fluorescence, Stabilité protéique, Urée.
English descriptors
- KwdEn :
- Binding Sites, Circular Dichroism, Coronavirus OC43, Human (chemistry), Glutaral (chemistry), Humans, Nucleic Acids (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Multimerization, Protein Stability, RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Spectrometry, Fluorescence, Urea (chemistry).
- MESH :
- chemical , chemistry : Glutaral, Nucleocapsid Proteins, RNA-Binding Proteins, Recombinant Proteins, Urea.
- chemistry : Coronavirus OC43, Human.
- chemical , metabolism : Nucleic Acids, Nucleocapsid Proteins, RNA-Binding Proteins, Recombinant Proteins.
- Binding Sites, Circular Dichroism, Humans, Protein Multimerization, Protein Stability, Spectrometry, Fluorescence.
Abstract
Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation.
DOI: 10.1002/pro.225
PubMed: 19691129
Affiliations:
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M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19691129</idno><idno type="pmid">19691129</idno><idno type="doi">10.1002/pro.225</idno><idno type="wicri:Area/PubMed/Corpus">001845</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001845</idno><idno type="wicri:Area/PubMed/Curation">001845</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001845</idno><idno type="wicri:Area/PubMed/Checkpoint">001885</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001885</idno><idno type="wicri:Area/Ncbi/Merge">001F84</idno><idno type="wicri:Area/Ncbi/Curation">001F84</idno><idno type="wicri:Area/Ncbi/Checkpoint">001F84</idno><idno type="wicri:Area/Main/Merge">002B78</idno><idno type="wicri:Area/Main/Curation">002B28</idno><idno type="wicri:Area/Main/Exploration">002B28</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.</title><author><name sortKey="Huang, Chun Yu" sort="Huang, Chun Yu" uniqKey="Huang C" first="Chun-Yu" last="Huang">Chun-Yu Huang</name><affiliation wicri:level="1"><nlm:affiliation>Biotechnology Center, National Chung Hsing University, Taichung 402, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>Biotechnology Center, National Chung Hsing University, Taichung 402</wicri:regionArea><wicri:noRegion>Taichung 402</wicri:noRegion></affiliation></author><author><name sortKey="Hsu, Yen Lan" sort="Hsu, Yen Lan" uniqKey="Hsu Y" first="Yen-Lan" last="Hsu">Yen-Lan Hsu</name></author><author><name sortKey="Chiang, Wan Ling" sort="Chiang, Wan Ling" uniqKey="Chiang W" first="Wan-Ling" last="Chiang">Wan-Ling Chiang</name></author><author><name sortKey="Hou, Ming Hon" sort="Hou, Ming Hon" uniqKey="Hou M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name></author></analytic><series><title level="j">Protein science : a publication of the Protein Society</title><idno type="eISSN">1469-896X</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Circular Dichroism</term><term>Coronavirus OC43, Human (chemistry)</term><term>Glutaral (chemistry)</term><term>Humans</term><term>Nucleic Acids (metabolism)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Multimerization</term><term>Protein Stability</term><term>RNA-Binding Proteins (chemistry)</term><term>RNA-Binding Proteins (metabolism)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Spectrometry, Fluorescence</term><term>Urea (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides nucléiques (métabolisme)</term><term>Coronavirus humain OC43 ()</term><term>Dichroïsme circulaire</term><term>Glutaraldéhyde ()</term><term>Humains</term><term>Multimérisation de protéines</term><term>Protéines de liaison à l'ARN ()</term><term>Protéines de liaison à l'ARN (métabolisme)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (métabolisme)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (métabolisme)</term><term>Sites de fixation</term><term>Spectrométrie de fluorescence</term><term>Stabilité protéique</term><term>Urée ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaral</term><term>Nucleocapsid Proteins</term><term>RNA-Binding Proteins</term><term>Recombinant Proteins</term><term>Urea</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronavirus OC43, Human</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleic Acids</term><term>Nucleocapsid Proteins</term><term>RNA-Binding Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides nucléiques</term><term>Protéines de liaison à l'ARN</term><term>Protéines nucléocapside</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Circular Dichroism</term><term>Humans</term><term>Protein Multimerization</term><term>Protein Stability</term><term>Spectrometry, Fluorescence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Coronavirus humain OC43</term><term>Dichroïsme circulaire</term><term>Glutaraldéhyde</term><term>Humains</term><term>Multimérisation de protéines</term><term>Protéines de liaison à l'ARN</term><term>Protéines nucléocapside</term><term>Protéines recombinantes</term><term>Sites de fixation</term><term>Spectrométrie de fluorescence</term><term>Stabilité protéique</term><term>Urée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation.</div></front></TEI><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Chiang, Wan Ling" sort="Chiang, Wan Ling" uniqKey="Chiang W" first="Wan-Ling" last="Chiang">Wan-Ling Chiang</name><name sortKey="Hou, Ming Hon" sort="Hou, Ming Hon" uniqKey="Hou M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name><name sortKey="Hsu, Yen Lan" sort="Hsu, Yen Lan" uniqKey="Hsu Y" first="Yen-Lan" last="Hsu">Yen-Lan Hsu</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Huang, Chun Yu" sort="Huang, Chun Yu" uniqKey="Huang C" first="Chun-Yu" last="Huang">Chun-Yu Huang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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