Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus.
Identifieur interne : 000F13 ( Ncbi/Merge ); précédent : 000F12; suivant : 000F14Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus.
Auteurs : Frank Qisheng Li [Singapour] ; Han Xiao ; James P. Tam ; D X LiuSource :
- FEBS letters [ 0014-5793 ] ; 2005.
Descripteurs français
- KwdFr :
- Cellules HeLa, Division cellulaire, Humains, Liaison aux protéines, Maturation post-traductionnelle des protéines, Petites protéines modificatrices apparentées à l'ubiquitine (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Protéines nucléocapside, Virus du SRAS.
- métabolisme : Petites protéines modificatrices apparentées à l'ubiquitine, Protéines nucléocapside, Virus du SRAS.
- Cellules HeLa, Division cellulaire, Humains, Liaison aux protéines, Maturation post-traductionnelle des protéines, Protéines nucléocapside.
English descriptors
- KwdEn :
- Cell Division, HeLa Cells, Humans, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Binding, Protein Processing, Post-Translational, SARS Virus (genetics), SARS Virus (metabolism), Small Ubiquitin-Related Modifier Proteins (metabolism).
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemical , genetics : Nucleocapsid Proteins.
- chemical , metabolism : Nucleocapsid Proteins, Small Ubiquitin-Related Modifier Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- Cell Division, HeLa Cells, Humans, Protein Binding, Protein Processing, Post-Translational.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes a highly basic nucleocapsid (N) protein of 422 amino acids. Similar to other coronavirus N proteins, SARS-CoV N protein is predicted to be phosphorylated and may contain nuclear localization signals, serine/arginine-rich motif, RNA binding domain and regions responsible for self-association and homo-oligomerization. In this study, we demonstrate that the protein is posttranslationally modified by covalent attachment to the small ubiquitin-like modifier. The major sumoylation site was mapped to the (62)lysine residue of the N protein. Further expression and characterization of wild type N protein and K62A mutant reveal that sumoylation of the N protein drastically promotes its homo-oligomerization, and plays certain roles in the N protein-mediated interference of host cell division. This is the first report showing that a coronavirus N protein undergoes posttranslational modification by sumoylation, and the functional implication of this modification in the formation of coronavirus ribouncleoprotein complex, virion assembly and virus-host interactions.
DOI: 10.1016/j.febslet.2005.03.039
PubMed: 15848177
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Tam</name></author><author><name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D X" last="Liu">D X Liu</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Division</term><term>HeLa Cells</term><term>Humans</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Processing, Post-Translational</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>Small Ubiquitin-Related Modifier Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HeLa</term><term>Division cellulaire</term><term>Humains</term><term>Liaison aux protéines</term><term>Maturation post-traductionnelle des protéines</term><term>Petites protéines modificatrices apparentées à l'ubiquitine (métabolisme)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (génétique)</term><term>Protéines nucléocapside (métabolisme)</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Small Ubiquitin-Related Modifier Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Petites protéines modificatrices apparentées à l'ubiquitine</term><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Division</term><term>HeLa Cells</term><term>Humans</term><term>Protein Binding</term><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term><term>Division cellulaire</term><term>Humains</term><term>Liaison aux protéines</term><term>Maturation post-traductionnelle des protéines</term><term>Protéines nucléocapside</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes a highly basic nucleocapsid (N) protein of 422 amino acids. Similar to other coronavirus N proteins, SARS-CoV N protein is predicted to be phosphorylated and may contain nuclear localization signals, serine/arginine-rich motif, RNA binding domain and regions responsible for self-association and homo-oligomerization. In this study, we demonstrate that the protein is posttranslationally modified by covalent attachment to the small ubiquitin-like modifier. The major sumoylation site was mapped to the (62)lysine residue of the N protein. Further expression and characterization of wild type N protein and K62A mutant reveal that sumoylation of the N protein drastically promotes its homo-oligomerization, and plays certain roles in the N protein-mediated interference of host cell division. This is the first report showing that a coronavirus N protein undergoes posttranslational modification by sumoylation, and the functional implication of this modification in the formation of coronavirus ribouncleoprotein complex, virion assembly and virus-host interactions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15848177</PMID><DateCompleted><Year>2005</Year><Month>05</Month><Day>31</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>579</Volume><Issue>11</Issue><PubDate><Year>2005</Year><Month>Apr</Month><Day>25</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett.</ISOAbbreviation></Journal><ArticleTitle>Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus.</ArticleTitle><Pagination><MedlinePgn>2387-96</MedlinePgn></Pagination><Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes a highly basic nucleocapsid (N) protein of 422 amino acids. Similar to other coronavirus N proteins, SARS-CoV N protein is predicted to be phosphorylated and may contain nuclear localization signals, serine/arginine-rich motif, RNA binding domain and regions responsible for self-association and homo-oligomerization. In this study, we demonstrate that the protein is posttranslationally modified by covalent attachment to the small ubiquitin-like modifier. The major sumoylation site was mapped to the (62)lysine residue of the N protein. Further expression and characterization of wild type N protein and K62A mutant reveal that sumoylation of the N protein drastically promotes its homo-oligomerization, and plays certain roles in the N protein-mediated interference of host cell division. This is the first report showing that a coronavirus N protein undergoes posttranslational modification by sumoylation, and the functional implication of this modification in the formation of coronavirus ribouncleoprotein complex, virion assembly and virus-host interactions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Frank Qisheng</ForeName><Initials>FQ</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xiao</LastName><ForeName>Han</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Tam</LastName><ForeName>James P</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>D X</ForeName><Initials>DX</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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IdType="pubmed">11682121</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Singapour</li></country></list><tree><noCountry><name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D X" last="Liu">D X Liu</name><name sortKey="Tam, James P" sort="Tam, James P" uniqKey="Tam J" first="James P" last="Tam">James P. Tam</name><name sortKey="Xiao, Han" sort="Xiao, Han" uniqKey="Xiao H" first="Han" last="Xiao">Han Xiao</name></noCountry><country name="Singapour"><noRegion><name sortKey="Li, Frank Qisheng" sort="Li, Frank Qisheng" uniqKey="Li F" first="Frank Qisheng" last="Li">Frank Qisheng Li</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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