SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system
Identifieur interne : 004416 ( Main/Exploration ); précédent : 004415; suivant : 004417SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system
Auteurs : ZHENG FAN [République populaire de Chine] ; YUE ZHUO [République populaire de Chine] ; XINYU TAN [République populaire de Chine] ; ZHI ZHOU [République populaire de Chine] ; JIANGANG YUAN [République populaire de Chine] ; BOQIN QIANG [République populaire de Chine] ; JINGHUA YAN [République populaire de Chine] ; XIAOZHONG PENG [République populaire de Chine] ; George F. Gao [République populaire de Chine]Source :
- Journal of medical virology [ 0146-6615 ] ; 2006.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Enzyme.
English descriptors
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 GK62EE in the N protein is not responsible for binding to hUbc9. Mutations of hUbc9 at the enzyme active site C93A or C93S severely impairthe 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.
Affiliations:
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<term>Nucléocapside</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<sup>62</sup>
EE in the N protein is not responsible for binding to hUbc9. Mutations of hUbc9 at the enzyme active site C93A or C93S severely impairthe 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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<name sortKey="Zhi Zhou" sort="Zhi Zhou" uniqKey="Zhi Zhou" last="Zhi Zhou">ZHI ZHOU</name>
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