The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases.
Identifieur interne : 003018 ( PubMed/Checkpoint ); précédent : 003017; suivant : 003019The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases.
Auteurs : Julian A. Tanner [République populaire de Chine] ; Rory M. Watt ; Yu-Bo Chai ; Lin-Yu Lu ; Marie C. Lin ; J S Malik Peiris ; Leo L M. Poon ; Hsiang-Fu Kung ; Jian-Dong HuangSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2003.
Descripteurs français
- KwdFr :
- ADN viral (génétique), ADN viral (métabolisme), Animaux, Cellules Vero, Cinétique, Données de séquences moléculaires, Helicase (), Helicase (génétique), Helicase (métabolisme), Nucleoside-triphosphatase (), Nucleoside-triphosphatase (génétique), Nucleoside-triphosphatase (métabolisme), RNA helicases (), RNA helicases (génétique), RNA helicases (métabolisme), Spécificité du substrat, Séquence nucléotidique, Virus du SRAS (enzymologie), Virus du SRAS (génétique).
- MESH :
- enzymologie : Virus du SRAS.
- génétique : ADN viral, Helicase, Nucleoside-triphosphatase, RNA helicases, Virus du SRAS.
- métabolisme : ADN viral, Helicase, Nucleoside-triphosphatase, RNA helicases.
- Animaux, Cellules Vero, Cinétique, Données de séquences moléculaires, Helicase, Nucleoside-triphosphatase, RNA helicases, Spécificité du substrat, Séquence nucléotidique.
English descriptors
- KwdEn :
- Animals, Base Sequence, Chlorocebus aethiops, DNA Helicases (classification), DNA Helicases (genetics), DNA Helicases (metabolism), DNA, Viral (genetics), DNA, Viral (metabolism), Kinetics, Molecular Sequence Data, Nucleoside-Triphosphatase (classification), Nucleoside-Triphosphatase (genetics), Nucleoside-Triphosphatase (metabolism), RNA Helicases (classification), RNA Helicases (genetics), RNA Helicases (metabolism), SARS Virus (enzymology), SARS Virus (genetics), Substrate Specificity, Vero Cells.
- MESH :
- chemical , classification : DNA Helicases, Nucleoside-Triphosphatase, RNA Helicases.
- chemical , genetics : DNA Helicases, DNA, Viral, Nucleoside-Triphosphatase, RNA Helicases.
- chemical , metabolism : DNA Helicases, DNA, Viral, Nucleoside-Triphosphatase, RNA Helicases.
- enzymology : SARS Virus.
- genetics : SARS Virus.
- Animals, Base Sequence, Chlorocebus aethiops, Kinetics, Molecular Sequence Data, Substrate Specificity, Vero Cells.
Abstract
The putative NTPase/helicase protein from severe acute respiratory syndrome coronavirus (SARS-CoV) is postulated to play a number of crucial roles in the viral life cycle, making it an attractive target for anti-SARS therapy. We have cloned, expressed, and purified this protein as an N-terminal hexahistidine fusion in Escherichia coli and have characterized its helicase and NTPase activities. The enzyme unwinds double-stranded DNA, dependent on the presence of a 5' single-stranded overhang, indicating a 5'o 3' polarity of activity, a distinct characteristic of coronaviridae helicases. We provide the first quantitative analysis of the polynucleic acid binding and NTPase activities of a Nidovirus helicase, using a high throughput phosphate release assay that will be readily adaptable to the future testing of helicase inhibitors. All eight common NTPs and dNTPs were hydrolyzed by the SARS helicase in a magnesium-dependent reaction, stimulated by the presence of either single-stranded DNA or RNA. The enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates. Homopolynucleotides significantly stimulated the ATPase activity (15-25-fold) with the notable exception of poly(G) and poly(dG), which were non-stimulatory. We found a large variation in the apparent strength of binding of different homopolynucleotides, with dT24 binding over 10 times more strongly than dA24 as observed by the apparent Km.
DOI: 10.1074/jbc.C300328200
PubMed: 12917423
Affiliations:
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We have cloned, expressed, and purified this protein as an N-terminal hexahistidine fusion in Escherichia coli and have characterized its helicase and NTPase activities. The enzyme unwinds double-stranded DNA, dependent on the presence of a 5' single-stranded overhang, indicating a 5'o 3' polarity of activity, a distinct characteristic of coronaviridae helicases. We provide the first quantitative analysis of the polynucleic acid binding and NTPase activities of a Nidovirus helicase, using a high throughput phosphate release assay that will be readily adaptable to the future testing of helicase inhibitors. All eight common NTPs and dNTPs were hydrolyzed by the SARS helicase in a magnesium-dependent reaction, stimulated by the presence of either single-stranded DNA or RNA. The enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates. Homopolynucleotides significantly stimulated the ATPase activity (15-25-fold) with the notable exception of poly(G) and poly(dG), which were non-stimulatory. We found a large variation in the apparent strength of binding of different homopolynucleotides, with dT24 binding over 10 times more strongly than dA24 as observed by the apparent Km.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12917423</PMID><DateCompleted><Year>2003</Year><Month>12</Month><Day>02</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>278</Volume><Issue>41</Issue><PubDate><Year>2003</Year><Month>Oct</Month><Day>10</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases.</ArticleTitle><Pagination><MedlinePgn>39578-82</MedlinePgn></Pagination><Abstract><AbstractText>The putative NTPase/helicase protein from severe acute respiratory syndrome coronavirus (SARS-CoV) is postulated to play a number of crucial roles in the viral life cycle, making it an attractive target for anti-SARS therapy. We have cloned, expressed, and purified this protein as an N-terminal hexahistidine fusion in Escherichia coli and have characterized its helicase and NTPase activities. The enzyme unwinds double-stranded DNA, dependent on the presence of a 5' single-stranded overhang, indicating a 5'o 3' polarity of activity, a distinct characteristic of coronaviridae helicases. We provide the first quantitative analysis of the polynucleic acid binding and NTPase activities of a Nidovirus helicase, using a high throughput phosphate release assay that will be readily adaptable to the future testing of helicase inhibitors. All eight common NTPs and dNTPs were hydrolyzed by the SARS helicase in a magnesium-dependent reaction, stimulated by the presence of either single-stranded DNA or RNA. The enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates. Homopolynucleotides significantly stimulated the ATPase activity (15-25-fold) with the notable exception of poly(G) and poly(dG), which were non-stimulatory. We found a large variation in the apparent strength of binding of different homopolynucleotides, with dT24 binding over 10 times more strongly than dA24 as observed by the apparent Km.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tanner</LastName><ForeName>Julian A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong Special Administrative Region, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Watt</LastName><ForeName>Rory M</ForeName><Initials>RM</Initials></Author><Author ValidYN="Y"><LastName>Chai</LastName><ForeName>Yu-Bo</ForeName><Initials>YB</Initials></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Lin-Yu</ForeName><Initials>LY</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Marie C</ForeName><Initials>MC</Initials></Author><Author ValidYN="Y"><LastName>Peiris</LastName><ForeName>J S Malik</ForeName><Initials>JS</Initials></Author><Author ValidYN="Y"><LastName>Poon</LastName><ForeName>Leo L M</ForeName><Initials>LL</Initials></Author><Author ValidYN="Y"><LastName>Kung</LastName><ForeName>Hsiang-Fu</ForeName><Initials>HF</Initials></Author><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Jian-Dong</ForeName><Initials>JD</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>RefSeq</DataBankName><AccessionNumberList><AccessionNumber>NC_828870</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2003</Year><Month>08</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004279">DNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.15</RegistryNumber><NameOfSubstance UI="D043583">Nucleoside-Triphosphatase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.4.-</RegistryNumber><NameOfSubstance UI="D004265">DNA Helicases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.4.13</RegistryNumber><NameOfSubstance UI="D020365">RNA Helicases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004265" MajorTopicYN="N">DNA Helicases</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004279" MajorTopicYN="N">DNA, Viral</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D043583" MajorTopicYN="N">Nucleoside-Triphosphatase</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020365" MajorTopicYN="N">RNA Helicases</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>8</Month><Day>15</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>12</Month><Day>3</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>8</Month><Day>15</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12917423</ArticleId><ArticleId IdType="doi">10.1074/jbc.C300328200</ArticleId><ArticleId IdType="pii">C300328200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Chai, Yu Bo" sort="Chai, Yu Bo" uniqKey="Chai Y" first="Yu-Bo" last="Chai">Yu-Bo Chai</name><name sortKey="Huang, Jian Dong" sort="Huang, Jian Dong" uniqKey="Huang J" first="Jian-Dong" last="Huang">Jian-Dong Huang</name><name sortKey="Kung, Hsiang Fu" sort="Kung, Hsiang Fu" uniqKey="Kung H" first="Hsiang-Fu" last="Kung">Hsiang-Fu Kung</name><name sortKey="Lin, Marie C" sort="Lin, Marie C" uniqKey="Lin M" first="Marie C" last="Lin">Marie C. Lin</name><name sortKey="Lu, Lin Yu" sort="Lu, Lin Yu" uniqKey="Lu L" first="Lin-Yu" last="Lu">Lin-Yu Lu</name><name sortKey="Peiris, J S Malik" sort="Peiris, J S Malik" uniqKey="Peiris J" first="J S Malik" last="Peiris">J S Malik Peiris</name><name sortKey="Poon, Leo L M" sort="Poon, Leo L M" uniqKey="Poon L" first="Leo L M" last="Poon">Leo L M. Poon</name><name sortKey="Watt, Rory M" sort="Watt, Rory M" uniqKey="Watt R" first="Rory M" last="Watt">Rory M. Watt</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Tanner, Julian A" sort="Tanner, Julian A" uniqKey="Tanner J" first="Julian A" last="Tanner">Julian A. Tanner</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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