Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP.
Identifieur interne : 001191 ( PubMed/Curation ); précédent : 001190; suivant : 001192Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP.
Auteurs : Xu Jin [République populaire de Chine] ; Yu Chen ; Ying Sun ; Cong Zeng ; Yi Wang ; Jiali Tao ; Andong Wu ; Xiao Yu ; Zhou Zhang ; Jie Tian ; Deyin GuoSource :
- Virus research [ 1872-7492 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Exoribonucleases, Guanosine Triphosphate, Methyltransferases, Viral Nonstructural Proteins.
- DNA Mutational Analysis, Substrate Specificity.
Abstract
Most eukaryotic viruses that replicate in the cytoplasm, including coronaviruses, have evolved strategies to cap their RNAs. In our previous work, the nonstructural protein (nsp) 14 of severe acute respiratory syndrome coronavirus (SARS-CoV) was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). In this study, we found that GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by SARS-CoV nsp14. In contrast, the nsp14 could not modify ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA. Critical residues of nsp14 essential for the methyltransferase activity on GTP were identified, which include F73, R84, W86, R310, D331, G333, P335, Y368, C414, and C416. We further showed that the methyltransferase activity of GTP was universal for nsp14 of other coronaviruses. Moreover, the accumulation of m7GTP or presence of protein nsp14 could interfere with protein translation of cellular mRNAs. Altogether, the results revealed a new enzymatic activity of coronavirus nsp14.
DOI: 10.1016/j.virusres.2013.05.001
PubMed: 23702198
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Zeng</name></author><author><name sortKey="Wang, Yi" sort="Wang, Yi" uniqKey="Wang Y" first="Yi" last="Wang">Yi Wang</name></author><author><name sortKey="Tao, Jiali" sort="Tao, Jiali" uniqKey="Tao J" first="Jiali" last="Tao">Jiali Tao</name></author><author><name sortKey="Wu, Andong" sort="Wu, Andong" uniqKey="Wu A" first="Andong" last="Wu">Andong Wu</name></author><author><name sortKey="Yu, Xiao" sort="Yu, Xiao" uniqKey="Yu X" first="Xiao" last="Yu">Xiao Yu</name></author><author><name sortKey="Zhang, Zhou" sort="Zhang, Zhou" uniqKey="Zhang Z" first="Zhou" last="Zhang">Zhou Zhang</name></author><author><name sortKey="Tian, Jie" sort="Tian, Jie" uniqKey="Tian J" first="Jie" last="Tian">Jie Tian</name></author><author><name sortKey="Guo, Deyin" sort="Guo, Deyin" uniqKey="Guo D" first="Deyin" last="Guo">Deyin Guo</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23702198</idno><idno 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430072</wicri:regionArea></affiliation></author><author><name sortKey="Chen, Yu" sort="Chen, Yu" uniqKey="Chen Y" first="Yu" last="Chen">Yu Chen</name></author><author><name sortKey="Sun, Ying" sort="Sun, Ying" uniqKey="Sun Y" first="Ying" last="Sun">Ying Sun</name></author><author><name sortKey="Zeng, Cong" sort="Zeng, Cong" uniqKey="Zeng C" first="Cong" last="Zeng">Cong Zeng</name></author><author><name sortKey="Wang, Yi" sort="Wang, Yi" uniqKey="Wang Y" first="Yi" last="Wang">Yi Wang</name></author><author><name sortKey="Tao, Jiali" sort="Tao, Jiali" uniqKey="Tao J" first="Jiali" last="Tao">Jiali Tao</name></author><author><name sortKey="Wu, Andong" sort="Wu, Andong" uniqKey="Wu A" first="Andong" last="Wu">Andong Wu</name></author><author><name sortKey="Yu, Xiao" sort="Yu, Xiao" uniqKey="Yu X" first="Xiao" last="Yu">Xiao Yu</name></author><author><name sortKey="Zhang, Zhou" sort="Zhang, Zhou" uniqKey="Zhang Z" first="Zhou" last="Zhang">Zhou Zhang</name></author><author><name sortKey="Tian, Jie" sort="Tian, Jie" uniqKey="Tian J" first="Jie" last="Tian">Jie Tian</name></author><author><name sortKey="Guo, Deyin" sort="Guo, Deyin" uniqKey="Guo D" first="Deyin" last="Guo">Deyin Guo</name></author></analytic><series><title level="j">Virus research</title><idno type="eISSN">1872-7492</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>DNA Mutational Analysis</term><term>Exoribonucleases (metabolism)</term><term>Guanosine Triphosphate (metabolism)</term><term>Methyltransferases (metabolism)</term><term>Substrate Specificity</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de mutations d'ADN</term><term>Exoribonucleases (métabolisme)</term><term>Guanosine triphosphate (métabolisme)</term><term>Methyltransferases (métabolisme)</term><term>Protéines virales non structurales (métabolisme)</term><term>Spécificité du substrat</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Exoribonucleases</term><term>Guanosine Triphosphate</term><term>Methyltransferases</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Exoribonucleases</term><term>Guanosine triphosphate</term><term>Methyltransferases</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>DNA Mutational Analysis</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de mutations d'ADN</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Most eukaryotic viruses that replicate in the cytoplasm, including coronaviruses, have evolved strategies to cap their RNAs. In our previous work, the nonstructural protein (nsp) 14 of severe acute respiratory syndrome coronavirus (SARS-CoV) was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). In this study, we found that GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by SARS-CoV nsp14. In contrast, the nsp14 could not modify ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA. Critical residues of nsp14 essential for the methyltransferase activity on GTP were identified, which include F73, R84, W86, R310, D331, G333, P335, Y368, C414, and C416. We further showed that the methyltransferase activity of GTP was universal for nsp14 of other coronaviruses. Moreover, the accumulation of m7GTP or presence of protein nsp14 could interfere with protein translation of cellular mRNAs. Altogether, the results revealed a new enzymatic activity of coronavirus nsp14.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23702198</PMID><DateCompleted><Year>2014</Year><Month>02</Month><Day>28</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-7492</ISSN><JournalIssue CitedMedium="Internet"><Volume>176</Volume><Issue>1-2</Issue><PubDate><Year>2013</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP.</ArticleTitle><Pagination><MedlinePgn>45-52</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virusres.2013.05.001</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0168-1702(13)00148-2</ELocationID><Abstract><AbstractText>Most eukaryotic viruses that replicate in the cytoplasm, including coronaviruses, have evolved strategies to cap their RNAs. In our previous work, the nonstructural protein (nsp) 14 of severe acute respiratory syndrome coronavirus (SARS-CoV) was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). In this study, we found that GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by SARS-CoV nsp14. In contrast, the nsp14 could not modify ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA. Critical residues of nsp14 essential for the methyltransferase activity on GTP were identified, which include F73, R84, W86, R310, D331, G333, P335, Y368, C414, and C416. We further showed that the methyltransferase activity of GTP was universal for nsp14 of other coronaviruses. Moreover, the accumulation of m7GTP or presence of protein nsp14 could interfere with protein translation of cellular mRNAs. Altogether, the results revealed a new enzymatic activity of coronavirus nsp14.</AbstractText><CopyrightInformation>Copyright © 2013 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Xu</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Yu</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Ying</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Zeng</LastName><ForeName>Cong</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yi</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Tao</LastName><ForeName>Jiali</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Andong</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Xiao</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Zhou</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Tian</LastName><ForeName>Jie</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Deyin</ForeName><Initials>D</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>2013</Year><Month>05</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Virus Res</MedlineTA><NlmUniqueID>8410979</NlmUniqueID><ISSNLinking>0168-1702</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral 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