Without Its N-Finger, the Main Protease of Severe Acute Respiratory Syndrome Coronavirus Can Form a Novel Dimer through Its C-Terminal Domain
Identifieur interne : 003457 ( Main/Curation ); précédent : 003456; suivant : 003458Without Its N-Finger, the Main Protease of Severe Acute Respiratory Syndrome Coronavirus Can Form a Novel Dimer through Its C-Terminal Domain
Auteurs : NAN ZHONG [République populaire de Chine] ; SHENGNAN ZHANG [République populaire de Chine] ; PENG ZOU [République populaire de Chine] ; JIAXUAN CHEN [République populaire de Chine] ; XUE KANG [République populaire de Chine] ; ZHE LI [République populaire de Chine] ; CHAO LIANG [République populaire de Chine] ; CHANGWEN JIN [République populaire de Chine] ; BIN XIA [République populaire de Chine]Source :
- Journal of virology [ 0022-538X ] ; 2008.
Descripteurs français
- Pascal (Inist)
English descriptors
Abstract
The main protease (Mpro) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing of the viral polyproteins (ppla and pplab), and it is an important target for anti-SARS drug development. It was found that SARS-CoV Mpro exists in solution as an equilibrium of both monomeric and dimeric forms, and the dimeric form is the enzymatically active form. However, the mechanism of SARS-CoV Mpro dimerization, especially the roles of its N-terminal seven residues (N-finger) and its unique C-terminal domain in the dimerization, remain unclear. Here we report that the SARS-CoV Mpro C-terminal domain alone (residues 187 to 306; Mpro-C) is produced in Escherichia coli in both monomeric and dimeric forms, and no exchange could be observed between them at room temperature. The Mpro-C dimer has a novel dimerization interface. Meanwhile, the N-finger deletion mutant of SARS-CoV Mpro also exists as both a stable monomer and a stable dimer, and the dimer is formed through the same C-terminal-domain interaction as that in the Mpro-C dimer. However, no C-terminal domain-mediated dimerization form can be detected for wild-type SARS-CoV Mpro. Our study results help to clarify previously published controversial claims about the role of the N-finger in SARS-CoV Mpro dimerization. Apparently, without the N-finger, SARS-CoV Mpro can no longer retain the active dimer structure; instead, it can form a new type of dimer which is inactive. Therefore, the N-finger of SARS-CoV Mpro is not only critical for its dimerization but also essential for the enzyme to form the enzymatically active dimer.
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Pascal:08-0228459Le document en format XML
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</inist:fA14>
<country>République populaire de Chine</country>
<placeName><settlement type="city">Pékin</settlement>
</placeName>
<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
<affiliation wicri:level="4"><inist:fA14 i1="02"><s1>College of Chemistry and Molecular Engineering, Peking University</s1>
<s2>Beijing 100871</s2>
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<placeName><settlement type="city">Pékin</settlement>
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<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Jiaxuan Chen" sort="Jiaxuan Chen" uniqKey="Jiaxuan Chen" last="Jiaxuan Chen">JIAXUAN CHEN</name>
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<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
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<placeName><settlement type="city">Pékin</settlement>
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</author>
<author><name sortKey="Xue Kang" sort="Xue Kang" uniqKey="Xue Kang" last="Xue Kang">XUE KANG</name>
<affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Beijing Nuclear Magnetic Resonance Center, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
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<placeName><settlement type="city">Pékin</settlement>
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<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
<affiliation wicri:level="4"><inist:fA14 i1="02"><s1>College of Chemistry and Molecular Engineering, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
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<country>République populaire de Chine</country>
<placeName><settlement type="city">Pékin</settlement>
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<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Zhe Li" sort="Zhe Li" uniqKey="Zhe Li" last="Zhe Li">ZHE LI</name>
<affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Beijing Nuclear Magnetic Resonance Center, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
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<region type="capitale">Pékin</region>
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</affiliation>
<affiliation wicri:level="4"><inist:fA14 i1="03"><s1>College of Life Science, Peking University</s1>
<s2>Beijing 100871</s2>
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<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Chao Liang" sort="Chao Liang" uniqKey="Chao Liang" last="Chao Liang">CHAO LIANG</name>
<affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Beijing Nuclear Magnetic Resonance Center, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
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<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Changwen Jin" sort="Changwen Jin" uniqKey="Changwen Jin" last="Changwen Jin">CHANGWEN JIN</name>
<affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Beijing Nuclear Magnetic Resonance Center, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
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<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
<affiliation wicri:level="4"><inist:fA14 i1="02"><s1>College of Chemistry and Molecular Engineering, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
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<country>République populaire de Chine</country>
<placeName><settlement type="city">Pékin</settlement>
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<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
<affiliation wicri:level="4"><inist:fA14 i1="03"><s1>College of Life Science, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
<sZ>4 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>8 aut.</sZ>
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</inist:fA14>
<country>République populaire de Chine</country>
<placeName><settlement type="city">Pékin</settlement>
</placeName>
<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Bin Xia" sort="Bin Xia" uniqKey="Bin Xia" last="Bin Xia">BIN XIA</name>
<affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Beijing Nuclear Magnetic Resonance Center, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
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<country>République populaire de Chine</country>
<placeName><settlement type="city">Pékin</settlement>
</placeName>
<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
<affiliation wicri:level="4"><inist:fA14 i1="02"><s1>College of Chemistry and Molecular Engineering, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
</inist:fA14>
<country>République populaire de Chine</country>
<placeName><settlement type="city">Pékin</settlement>
</placeName>
<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
<affiliation wicri:level="4"><inist:fA14 i1="03"><s1>College of Life Science, Peking University</s1>
<s2>Beijing 100871</s2>
<s3>CHN</s3>
<sZ>4 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
</inist:fA14>
<country>République populaire de Chine</country>
<placeName><settlement type="city">Pékin</settlement>
</placeName>
<orgName type="university">Université de Pékin</orgName>
<placeName><settlement type="city">Pékin</settlement>
<region type="capitale">Pékin</region>
</placeName>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date when="2008">2008</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term>
<term>Severe acute respiratory syndrome</term>
<term>Virology</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term>
<term>Virologie</term>
<term>Syndrome respiratoire aigu sévère</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The main protease (M<sup>pro</sup>
) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing of the viral polyproteins (ppla and pplab), and it is an important target for anti-SARS drug development. It was found that SARS-CoV M<sup>pro</sup>
exists in solution as an equilibrium of both monomeric and dimeric forms, and the dimeric form is the enzymatically active form. However, the mechanism of SARS-CoV M<sup>pro</sup>
dimerization, especially the roles of its N-terminal seven residues (N-finger) and its unique C-terminal domain in the dimerization, remain unclear. Here we report that the SARS-CoV M<sup>pro</sup>
C-terminal domain alone (residues 187 to 306; M<sup>pro</sup>
-C) is produced in Escherichia coli in both monomeric and dimeric forms, and no exchange could be observed between them at room temperature. The M<sup>pro</sup>
-C dimer has a novel dimerization interface. Meanwhile, the N-finger deletion mutant of SARS-CoV M<sup>pro</sup>
also exists as both a stable monomer and a stable dimer, and the dimer is formed through the same C-terminal-domain interaction as that in the M<sup>pro</sup>
-C dimer. However, no C-terminal domain-mediated dimerization form can be detected for wild-type SARS-CoV M<sup>pro</sup>
. Our study results help to clarify previously published controversial claims about the role of the N-finger in SARS-CoV M<sup>pro</sup>
dimerization. Apparently, without the N-finger, SARS-CoV M<sup>pro</sup>
can no longer retain the active dimer structure; instead, it can form a new type of dimer which is inactive. Therefore, the N-finger of SARS-CoV M<sup>pro</sup>
is not only critical for its dimerization but also essential for the enzyme to form the enzymatically active dimer.</div>
</front>
</TEI>
</record>
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