Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode.
Identifieur interne : 002275 ( Ncbi/Merge ); précédent : 002274; suivant : 002276Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode.
Auteurs : Shuai Chen [Allemagne] ; Felix Jonas ; Can Shen ; Rolf Hilgenfeld ; Rolf HigenfeldSource :
- Protein & cell [ 1674-8018 ] ; 2010.
Descripteurs français
- KwdFr :
- Chromatographie, Cysteine endopeptidases (), Cysteine endopeptidases (génétique), Cysteine endopeptidases (métabolisme), Dichroïsme circulaire, Multimérisation de protéines, Mutagenèse dirigée, Polyprotéines (), Polyprotéines (génétique), Polyprotéines (métabolisme), Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Spectrométrie de fluorescence, Virus du SRAS (), Virus du SRAS (enzymologie), Virus du SRAS (génétique).
- MESH :
- enzymologie : Virus du SRAS.
- génétique : Cysteine endopeptidases, Polyprotéines, Protéines virales, Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Polyprotéines, Protéines virales.
- Chromatographie, Cysteine endopeptidases, Dichroïsme circulaire, Multimérisation de protéines, Mutagenèse dirigée, Polyprotéines, Protéines virales, Spectrométrie de fluorescence, Virus du SRAS.
English descriptors
- KwdEn :
- Chromatography, Circular Dichroism, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Mutagenesis, Site-Directed, Polyproteins (chemistry), Polyproteins (genetics), Polyproteins (metabolism), Protein Multimerization, SARS Virus (chemistry), SARS Virus (enzymology), SARS Virus (genetics), Spectrometry, Fluorescence, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Polyproteins, Viral Proteins.
- chemical , genetics : Cysteine Endopeptidases, Polyproteins, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Polyproteins, Viral Proteins.
- chemistry : SARS Virus.
- enzymology : SARS Virus.
- genetics : SARS Virus.
- Chromatography, Circular Dichroism, Mutagenesis, Site-Directed, Protein Multimerization, Spectrometry, Fluorescence.
Abstract
The main protease (M(pro)) plays a vital role in proteolytic processing of the polyproteins in the replicative cycle of SARS coronavirus (SARS-CoV). Dimerization of this enzyme has been shown to be indispensable for trans-cleavage activity. However, the auto-processing mechanism of M(pro), i.e. its own release from the polyproteins through autocleavage, remains unclear. This study elucidates the relationship between the N-terminal autocleavage activity and the dimerization of "immature" M(pro). Three residues (Arg4, Glu290, and Arg298), which contribute to the active dimer conformation of mature M(pro), are selected for mutational analyses. Surprisingly, all three mutants still perform N-terminal autocleavage, while the dimerization of mature protease and trans-cleavage activity following auto-processing are completely inhibited by the E290R and R298E mutations and partially so by the R4E mutation. Furthermore, the mature E290R mutant can resume N-terminal autocleavage activity when mixed with the "immature" C145A/E290R double mutant whereas its trans-cleavage activity remains absent. Therefore, the N-terminal auto-processing of M(pro) appears to require only two "immature" monomers approaching one another to form an "intermediate" dimer structure and does not strictly depend on the active dimer conformation existing in mature protease. In conclusion, an auto-release model of M(pro) from the polyproteins is proposed, which will help understand the auto-processing mechanism and the difference between the autocleavage and trans-cleavage proteolytic activities of SARS-CoV M(pro).
DOI: 10.1007/s13238-010-0011-4
PubMed: 21203998
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001567
- to stream PubMed, to step Curation: 001567
- to stream PubMed, to step Checkpoint: 001637
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pubmed:21203998Le document en format XML
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Lübeck</wicri:noRegion><wicri:noRegion>23538 Lübeck</wicri:noRegion><wicri:noRegion>23538 Lübeck</wicri:noRegion></affiliation></author><author><name sortKey="Jonas, Felix" sort="Jonas, Felix" uniqKey="Jonas F" first="Felix" last="Jonas">Felix Jonas</name></author><author><name sortKey="Shen, Can" sort="Shen, Can" uniqKey="Shen C" first="Can" last="Shen">Can Shen</name></author><author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name></author><author><name sortKey="Higenfeld, Rolf" sort="Higenfeld, Rolf" uniqKey="Higenfeld R" first="Rolf" last="Higenfeld">Rolf Higenfeld</name></author></analytic><series><title level="j">Protein & cell</title><idno type="eISSN">1674-8018</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography</term><term>Circular 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(génétique)</term><term>Polyprotéines (métabolisme)</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Protéines virales (métabolisme)</term><term>Spectrométrie de fluorescence</term><term>Virus du SRAS ()</term><term>Virus du SRAS (enzymologie)</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Polyproteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Polyproteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Polyproteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Polyprotéines</term><term>Protéines virales</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Polyprotéines</term><term>Protéines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography</term><term>Circular Dichroism</term><term>Mutagenesis, Site-Directed</term><term>Protein Multimerization</term><term>Spectrometry, Fluorescence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie</term><term>Cysteine endopeptidases</term><term>Dichroïsme circulaire</term><term>Multimérisation de protéines</term><term>Mutagenèse dirigée</term><term>Polyprotéines</term><term>Protéines virales</term><term>Spectrométrie de fluorescence</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The main protease (M(pro)) plays a vital role in proteolytic processing of the polyproteins in the replicative cycle of SARS coronavirus (SARS-CoV). Dimerization of this enzyme has been shown to be indispensable for trans-cleavage activity. However, the auto-processing mechanism of M(pro), i.e. its own release from the polyproteins through autocleavage, remains unclear. This study elucidates the relationship between the N-terminal autocleavage activity and the dimerization of "immature" M(pro). Three residues (Arg4, Glu290, and Arg298), which contribute to the active dimer conformation of mature M(pro), are selected for mutational analyses. Surprisingly, all three mutants still perform N-terminal autocleavage, while the dimerization of mature protease and trans-cleavage activity following auto-processing are completely inhibited by the E290R and R298E mutations and partially so by the R4E mutation. Furthermore, the mature E290R mutant can resume N-terminal autocleavage activity when mixed with the "immature" C145A/E290R double mutant whereas its trans-cleavage activity remains absent. Therefore, the N-terminal auto-processing of M(pro) appears to require only two "immature" monomers approaching one another to form an "intermediate" dimer structure and does not strictly depend on the active dimer conformation existing in mature protease. In conclusion, an auto-release model of M(pro) from the polyproteins is proposed, which will help understand the auto-processing mechanism and the difference between the autocleavage and trans-cleavage proteolytic activities of SARS-CoV M(pro).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21203998</PMID><DateCompleted><Year>2011</Year><Month>04</Month><Day>27</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1674-8018</ISSN><JournalIssue CitedMedium="Internet"><Volume>1</Volume><Issue>1</Issue><PubDate><Year>2010</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Protein & cell</Title><ISOAbbreviation>Protein Cell</ISOAbbreviation></Journal><ArticleTitle>Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode.</ArticleTitle><Pagination><MedlinePgn>59-74</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s13238-010-0011-4</ELocationID><Abstract><AbstractText>The main protease (M(pro)) plays a vital role in proteolytic processing of the polyproteins in the replicative cycle of SARS coronavirus (SARS-CoV). Dimerization of this enzyme has been shown to be indispensable for trans-cleavage activity. However, the auto-processing mechanism of M(pro), i.e. its own release from the polyproteins through autocleavage, remains unclear. This study elucidates the relationship between the N-terminal autocleavage activity and the dimerization of "immature" M(pro). Three residues (Arg4, Glu290, and Arg298), which contribute to the active dimer conformation of mature M(pro), are selected for mutational analyses. Surprisingly, all three mutants still perform N-terminal autocleavage, while the dimerization of mature protease and trans-cleavage activity following auto-processing are completely inhibited by the E290R and R298E mutations and partially so by the R4E mutation. Furthermore, the mature E290R mutant can resume N-terminal autocleavage activity when mixed with the "immature" C145A/E290R double mutant whereas its trans-cleavage activity remains absent. Therefore, the N-terminal auto-processing of M(pro) appears to require only two "immature" monomers approaching one another to form an "intermediate" dimer structure and does not strictly depend on the active dimer conformation existing in mature protease. In conclusion, an auto-release model of M(pro) from the polyproteins is proposed, which will help understand the auto-processing mechanism and the difference between the autocleavage and trans-cleavage proteolytic activities of SARS-CoV M(pro).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Shuai</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jonas</LastName><ForeName>Felix</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Can</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Hilgenfeld</LastName><ForeName>Rolf</ForeName><Initials>R</Initials></Author><Author ValidYN="N"><LastName>Higenfeld</LastName><ForeName>Rolf</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>02</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Protein Cell</MedlineTA><NlmUniqueID>101532368</NlmUniqueID><ISSNLinking>1674-800X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020815">Polyproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="C099456">3C-like proteinase, 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020815" MajorTopicYN="N">Polyproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>10</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>11</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>1</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>1</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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