SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system
Identifieur interne : 000536 ( PascalFrancis/Curation ); précédent : 000535; suivant : 000537SARS-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.
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Gao</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Center for Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>7 aut.</sZ><sZ>9 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">INIST</idno><idno type="inist">06-0482826</idno><date when="2006">2006</date><idno type="stanalyst">PASCAL 06-0482826 INIST</idno><idno type="RBID">Pascal:06-0482826</idno><idno type="wicri:Area/PascalFrancis/Corpus">000454</idno><idno type="wicri:Area/PascalFrancis/Curation">000536</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system</title><author><name sortKey="Zheng Fan" sort="Zheng Fan" uniqKey="Zheng Fan" last="Zheng Fan">ZHENG FAN</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Center for Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>7 aut.</sZ><sZ>9 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Yue Zhuo" sort="Yue Zhuo" uniqKey="Yue Zhuo" last="Yue Zhuo">YUE ZHUO</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Center for Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>7 aut.</sZ><sZ>9 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Biochemistry, Anhui Agricultural University</s1><s2>Hefei</s2><s3>CHN</s3><sZ>2 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Xinyu Tan" sort="Xinyu Tan" uniqKey="Xinyu Tan" last="Xinyu Tan">XINYU TAN</name><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College</s1><s2>Beijing</s2><s3>CHN</s3><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Zhi Zhou" sort="Zhi Zhou" uniqKey="Zhi Zhou" last="Zhi Zhou">ZHI ZHOU</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Center for Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>7 aut.</sZ><sZ>9 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation><affiliation wicri:level="1"><inist:fA14 i1="04"><s1>College of Veterinary Medicine, China Agricultural University</s1><s2>Beijing</s2><s3>CHN</s3><sZ>4 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Jiangang Yuan" sort="Jiangang Yuan" uniqKey="Jiangang Yuan" last="Jiangang Yuan">JIANGANG YUAN</name><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College</s1><s2>Beijing</s2><s3>CHN</s3><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Boqin Qiang" sort="Boqin Qiang" uniqKey="Boqin Qiang" last="Boqin Qiang">BOQIN QIANG</name><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College</s1><s2>Beijing</s2><s3>CHN</s3><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Jinghua Yan" sort="Jinghua Yan" uniqKey="Jinghua Yan" last="Jinghua Yan">JINGHUA YAN</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Center for Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>7 aut.</sZ><sZ>9 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Xiaozhong Peng" sort="Xiaozhong Peng" uniqKey="Xiaozhong Peng" last="Xiaozhong Peng">XIAOZHONG PENG</name><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College</s1><s2>Beijing</s2><s3>CHN</s3><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author><author><name sortKey="Gao, George F" sort="Gao, George F" uniqKey="Gao G" first="George F." last="Gao">George F. Gao</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Center for Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>7 aut.</sZ><sZ>9 aut.</sZ></inist:fA14><country>République populaire de Chine</country></affiliation></author></analytic><series><title level="j" type="main">Journal of medical virology</title><title level="j" type="abbreviated">J. med. virol.</title><idno type="ISSN">0146-6615</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of medical virology</title><title level="j" type="abbreviated">J. med. virol.</title><idno type="ISSN">0146-6615</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term><term>Enzyme</term><term>Nucleocapsid</term><term>Protein</term><term>Severe acute respiratory syndrome</term><term>Ubiquitin</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term><term>Nucléocapside</term><term>Protéine</term><term>Ubiquitine</term><term>Enzyme</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Enzyme</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0146-6615</s0></fA01><fA02 i1="01"><s0>JMVIDB</s0></fA02><fA03 i2="1"><s0>J. med. virol.</s0></fA03><fA05><s2>78</s2></fA05><fA06><s2>11</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system</s1></fA08><fA11 i1="01" i2="1"><s1>ZHENG FAN</s1></fA11><fA11 i1="02" i2="1"><s1>YUE ZHUO</s1></fA11><fA11 i1="03" i2="1"><s1>XINYU TAN</s1></fA11><fA11 i1="04" i2="1"><s1>ZHI ZHOU</s1></fA11><fA11 i1="05" i2="1"><s1>JIANGANG YUAN</s1></fA11><fA11 i1="06" i2="1"><s1>BOQIN QIANG</s1></fA11><fA11 i1="07" i2="1"><s1>JINGHUA YAN</s1></fA11><fA11 i1="08" i2="1"><s1>XIAOZHONG PENG</s1></fA11><fA11 i1="09" i2="1"><s1>GAO (George F.)</s1></fA11><fA14 i1="01"><s1>Center for Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>7 aut.</sZ><sZ>9 aut.</sZ></fA14><fA14 i1="02"><s1>Department of Biochemistry, Anhui Agricultural University</s1><s2>Hefei</s2><s3>CHN</s3><sZ>2 aut.</sZ></fA14><fA14 i1="03"><s1>National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College</s1><s2>Beijing</s2><s3>CHN</s3><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></fA14><fA14 i1="04"><s1>College of Veterinary Medicine, China Agricultural University</s1><s2>Beijing</s2><s3>CHN</s3><sZ>4 aut.</sZ></fA14><fA20><s1>1365-1373</s1></fA20><fA21><s1>2006</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>17422</s2><s5>354000157221510010</s5></fA43><fA44><s0>0000</s0><s1>© 2006 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>29 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>06-0482826</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of medical virology</s0></fA64><fA66 i1="01"><s0>USA</s0></fA66><fC01 i1="01" l="ENG"><s0>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.</s0></fC01><fC02 i1="01" i2="X"><s0>002A05C10</s0></fC02><fC02 i1="02" i2="X"><s0>002B05C02J</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Nucléocapside</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Nucleocapsid</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Nucleocápside</s0><s5>05</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Protéine</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Protein</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Proteína</s0><s5>06</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Ubiquitine</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Ubiquitin</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Ubiquitina</s0><s5>07</s5></fC03><fC03 i1="05" i2="X" l="FRE"><s0>Enzyme</s0><s2>FE</s2><s5>08</s5></fC03><fC03 i1="05" i2="X" l="ENG"><s0>Enzyme</s0><s2>FE</s2><s5>08</s5></fC03><fC03 i1="05" i2="X" l="SPA"><s0>Enzima</s0><s2>FE</s2><s5>08</s5></fC03><fC03 i1="06" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="06" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="06" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0><s2>NM</s2><s5>14</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Appareil respiratoire pathologie</s0><s5>13</s5></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Respiratory disease</s0><s5>13</s5></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0><s5>13</s5></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Virose</s0></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Viral disease</s0></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Virosis</s0></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Infection</s0></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Infection</s0></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Infección</s0></fC07><fC07 i1="07" i2="X" l="FRE"><s0>Poumon pathologie</s0><s5>16</s5></fC07><fC07 i1="07" i2="X" l="ENG"><s0>Lung disease</s0><s5>16</s5></fC07><fC07 i1="07" i2="X" l="SPA"><s0>Pulmón patología</s0><s5>16</s5></fC07><fN21><s1>317</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard></inist></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Sante
|area= SrasV1
|flux= PascalFrancis
|étape= Curation
|type= RBID
|clé= Pascal:06-0482826
|texte= SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system
}}
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