Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.
Identifieur interne : 001265 ( PubMed/Corpus ); précédent : 001264; suivant : 001266Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.
Auteurs : A O Adedeji ; K. Singh ; S G SarafianosSource :
- Cellular and molecular biology (Noisy-le-Grand, France) [ 1165-158X ] ; 2012.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : DNA Helicases.
- chemical , genetics : DNA Helicases.
- chemical , metabolism : Adenosine Triphosphate, DNA Helicases, Nucleic Acids.
- enzymology : SARS Virus.
- Protein Binding.
Abstract
The non—structural protein 13 (nsp13) of Severe Acute Respiratory Syndrome Coronavirus (SARS—CoV) is a helicase that separates double—stranded RNA or DNA with a 5'—3' polarity, using the energy of nucleotide hydrolysis. We have previously determined the minimal mechanism of helicase function by nsp13 where we demonstrated that the enzyme unwinds nucleic acid in discrete steps of 9.3 base—pairs each with a catalytic rate of 30 steps per second. In that study we used different constructs of nsp13 (GST and H6 constructs). GST—nsp13 showed much more efficient nucleic acid unwinding than the H6—tagged counterpart. At 0.1 second, more than 50% of the ATP is hydrolyzed by GST—nsp13 compared to less than 5% ATP hydrolysis by H6—nsp13. Interestingly, the two constructs have the same binding affinity for nucleic acids. We, therefore propose that the difference in the catalytic efficiency of these two constructs is due to the interference of ATP binding by the histidine tag at the amino—terminus of nsp13.
PubMed: 23273200
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pubmed:23273200Le document en format XML
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Singh</name></author><author><name sortKey="Sarafianos, S G" sort="Sarafianos, S G" uniqKey="Sarafianos S" first="S G" last="Sarafianos">S G Sarafianos</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:23273200</idno><idno type="pmid">23273200</idno><idno type="wicri:Area/PubMed/Corpus">001265</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001265</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.</title><author><name sortKey="Adedeji, A O" sort="Adedeji, A O" uniqKey="Adedeji A" first="A O" last="Adedeji">A O Adedeji</name><affiliation><nlm:affiliation>Christopher S. Bond Life Sciences Center, University of Missouri School of Medicine, Columbia, MO 65211, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Singh, K" sort="Singh, K" uniqKey="Singh K" first="K" last="Singh">K. Singh</name></author><author><name sortKey="Sarafianos, S G" sort="Sarafianos, S G" uniqKey="Sarafianos S" first="S G" last="Sarafianos">S G Sarafianos</name></author></analytic><series><title level="j">Cellular and molecular biology (Noisy-le-Grand, France)</title><idno type="eISSN">1165-158X</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphate (metabolism)</term><term>DNA Helicases (chemistry)</term><term>DNA Helicases (genetics)</term><term>DNA Helicases (metabolism)</term><term>Nucleic Acids (metabolism)</term><term>Protein Binding</term><term>SARS Virus (enzymology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA Helicases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Helicases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphate</term><term>DNA Helicases</term><term>Nucleic Acids</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Binding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The non—structural protein 13 (nsp13) of Severe Acute Respiratory Syndrome Coronavirus (SARS—CoV) is a helicase that separates double—stranded RNA or DNA with a 5'—3' polarity, using the energy of nucleotide hydrolysis. We have previously determined the minimal mechanism of helicase function by nsp13 where we demonstrated that the enzyme unwinds nucleic acid in discrete steps of 9.3 base—pairs each with a catalytic rate of 30 steps per second. In that study we used different constructs of nsp13 (GST and H6 constructs). GST—nsp13 showed much more efficient nucleic acid unwinding than the H6—tagged counterpart. At 0.1 second, more than 50% of the ATP is hydrolyzed by GST—nsp13 compared to less than 5% ATP hydrolysis by H6—nsp13. Interestingly, the two constructs have the same binding affinity for nucleic acids. We, therefore propose that the difference in the catalytic efficiency of these two constructs is due to the interference of ATP binding by the histidine tag at the amino—terminus of nsp13.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23273200</PMID><DateCompleted><Year>2013</Year><Month>06</Month><Day>04</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1165-158X</ISSN><JournalIssue CitedMedium="Internet"><Volume>58</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Dec</Month><Day>22</Day></PubDate></JournalIssue><Title>Cellular and molecular biology (Noisy-le-Grand, France)</Title><ISOAbbreviation>Cell. Mol. Biol. (Noisy-le-grand)</ISOAbbreviation></Journal><ArticleTitle>Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.</ArticleTitle><Pagination><MedlinePgn>114-21</MedlinePgn></Pagination><Abstract><AbstractText>The non—structural protein 13 (nsp13) of Severe Acute Respiratory Syndrome Coronavirus (SARS—CoV) is a helicase that separates double—stranded RNA or DNA with a 5'—3' polarity, using the energy of nucleotide hydrolysis. We have previously determined the minimal mechanism of helicase function by nsp13 where we demonstrated that the enzyme unwinds nucleic acid in discrete steps of 9.3 base—pairs each with a catalytic rate of 30 steps per second. In that study we used different constructs of nsp13 (GST and H6 constructs). GST—nsp13 showed much more efficient nucleic acid unwinding than the H6—tagged counterpart. At 0.1 second, more than 50% of the ATP is hydrolyzed by GST—nsp13 compared to less than 5% ATP hydrolysis by H6—nsp13. Interestingly, the two constructs have the same binding affinity for nucleic acids. We, therefore propose that the difference in the catalytic efficiency of these two constructs is due to the interference of ATP binding by the histidine tag at the amino—terminus of nsp13.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Adedeji</LastName><ForeName>A O</ForeName><Initials>AO</Initials><AffiliationInfo><Affiliation>Christopher S. Bond Life Sciences Center, University of Missouri School of Medicine, Columbia, MO 65211, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Singh</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Sarafianos</LastName><ForeName>S G</ForeName><Initials>SG</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI074389</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R33 AI079801</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI079801</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI094715</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI074389</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 AI079801</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI076119</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 AI094715</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI100890</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI076119</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>12</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Cell Mol Biol (Noisy-le-grand)</MedlineTA><NlmUniqueID>9216789</NlmUniqueID><ISSNLinking>0145-5680</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009696">Nucleic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>8L70Q75FXE</RegistryNumber><NameOfSubstance UI="D000255">Adenosine Triphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.4.-</RegistryNumber><NameOfSubstance UI="D004265">DNA Helicases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000255" MajorTopicYN="N">Adenosine Triphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004265" MajorTopicYN="N">DNA 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