SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system.
Identifieur interne : 002020 ( PubMed/Checkpoint ); précédent : 002019; suivant : 002021SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system.
Auteurs : Zheng Fan [République populaire de Chine] ; Yue Zhuo ; Xinyu Tan ; Zhi Zhou ; Jiangang Yuan ; Boqin Qiang ; Jinghua Yan ; Xiaozhong Peng ; George F. GaoSource :
- Journal of medical virology [ 0146-6615 ] ; 2006.
Descripteurs français
- KwdFr :
- Humains, Liaison aux protéines, Lignée cellulaire, Petites protéines modificatrices apparentées à l'ubiquitine (métabolisme), Protéines nucléocapside (métabolisme), Sites de fixation, Techniques de double hybride, Ubiquitin-conjugating enzymes (métabolisme), Ubiquitine (métabolisme), Virus du SRAS (métabolisme).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Nucleocapsid Proteins, Small Ubiquitin-Related Modifier Proteins, Ubiquitin, Ubiquitin-Conjugating Enzymes.
- metabolism : SARS Virus.
- Binding Sites, Cell Line, Humans, Protein Binding, Two-Hybrid System Techniques.
Abstract
SARS-CoV is a newly identified coronavirus (CoV) that causes severe acute respiratory syndrome (SARS). The SARS-CoV nucleocapsid (N) protein is an important structural and functional protein. To identify cellular proteins that interact with the SARS-CoV N protein and to elucidate the possible involvement of N protein in SARS-CoV pathogenesis, a human lymphocyte cDNA library was screened using a yeast two-hybrid system assay. hUbc9, a ubiquitin conjugating enzyme of sumoylation system, was found to interact specifically with the N protein, implying the post-translational sumoylation of the N protein. Mapping studies localized the critical N sequences for this interaction to amino acids 170-210, which includes the SR-rich motif. However, the consensus motif of sumoylation GK(62)EE in the N protein is not responsible for binding to hUbc9. Mutations of hUbc9 at the enzyme active site C93A or C93S severely impair the interaction with the N protein. The two proteins were also shown to colocalize in the cytoplasm of the transfected 293T cells. This is the first report demonstrating the interaction of hUbc9 with a structural protein of plus-strand RNA viruses, indicating a new drug target for SARS-CoV.
DOI: 10.1002/jmv.20707
PubMed: 16998888
Affiliations:
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pubmed:16998888Le document en format XML
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<term>Lignée cellulaire</term>
<term>Sites de fixation</term>
<term>Techniques de double hybride</term>
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<front><div type="abstract" xml:lang="en">SARS-CoV is a newly identified coronavirus (CoV) that causes severe acute respiratory syndrome (SARS). The SARS-CoV nucleocapsid (N) protein is an important structural and functional protein. To identify cellular proteins that interact with the SARS-CoV N protein and to elucidate the possible involvement of N protein in SARS-CoV pathogenesis, a human lymphocyte cDNA library was screened using a yeast two-hybrid system assay. hUbc9, a ubiquitin conjugating enzyme of sumoylation system, was found to interact specifically with the N protein, implying the post-translational sumoylation of the N protein. Mapping studies localized the critical N sequences for this interaction to amino acids 170-210, which includes the SR-rich motif. However, the consensus motif of sumoylation GK(62)EE in the N protein is not responsible for binding to hUbc9. Mutations of hUbc9 at the enzyme active site C93A or C93S severely impair the interaction with the N protein. The two proteins were also shown to colocalize in the cytoplasm of the transfected 293T cells. This is the first report demonstrating the interaction of hUbc9 with a structural protein of plus-strand RNA viruses, indicating a new drug target for SARS-CoV.</div>
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<Abstract><AbstractText>SARS-CoV is a newly identified coronavirus (CoV) that causes severe acute respiratory syndrome (SARS). The SARS-CoV nucleocapsid (N) protein is an important structural and functional protein. To identify cellular proteins that interact with the SARS-CoV N protein and to elucidate the possible involvement of N protein in SARS-CoV pathogenesis, a human lymphocyte cDNA library was screened using a yeast two-hybrid system assay. hUbc9, a ubiquitin conjugating enzyme of sumoylation system, was found to interact specifically with the N protein, implying the post-translational sumoylation of the N protein. Mapping studies localized the critical N sequences for this interaction to amino acids 170-210, which includes the SR-rich motif. However, the consensus motif of sumoylation GK(62)EE in the N protein is not responsible for binding to hUbc9. Mutations of hUbc9 at the enzyme active site C93A or C93S severely impair the interaction with the N protein. The two proteins were also shown to colocalize in the cytoplasm of the transfected 293T cells. This is the first report demonstrating the interaction of hUbc9 with a structural protein of plus-strand RNA viruses, indicating a new drug target for SARS-CoV.</AbstractText>
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