The Inhibitory Effect of Non-Substrate and Substrate DNA on the Ligation and Self-Adenylylation Reactions Catalyzed by T4 DNA Ligase
Identifieur interne : 001001 ( Main/Exploration ); précédent : 001000; suivant : 001002The Inhibitory Effect of Non-Substrate and Substrate DNA on the Ligation and Self-Adenylylation Reactions Catalyzed by T4 DNA Ligase
Auteurs : Robert J. Bauer ; Thomas C. Evans ; Gregory J. S. LohmanSource :
- PLoS ONE [ 1932-6203 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : DNA, DNA Ligases.
- Catalysis, DNA Replication, In Vitro Techniques, Kinetics.
Abstract
DNA ligases are essential both to
Url:
DOI: 10.1371/journal.pone.0150802
PubMed: 26954034
PubMed Central: 4782999
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Inhibitory Effect of Non-Substrate and Substrate DNA on the Ligation and Self-Adenylylation Reactions Catalyzed by T4 DNA Ligase</title><author><name sortKey="Bauer, Robert J" sort="Bauer, Robert J" uniqKey="Bauer R" first="Robert J." last="Bauer">Robert J. Bauer</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Evans, Thomas C" sort="Evans, Thomas C" uniqKey="Evans T" first="Thomas C." last="Evans">Thomas C. Evans</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Lohman, Gregory J S" sort="Lohman, Gregory J S" uniqKey="Lohman G" first="Gregory J. S." last="Lohman">Gregory J. S. Lohman</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">26954034</idno><idno type="pmc">4782999</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4782999</idno><idno type="RBID">PMC:4782999</idno><idno type="doi">10.1371/journal.pone.0150802</idno><date when="2016">2016</date><idno type="wicri:Area/Pmc/Corpus">001023</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001023</idno><idno type="wicri:Area/Pmc/Curation">001023</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001023</idno><idno type="wicri:Area/Pmc/Checkpoint">000989</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000989</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:26954034</idno><idno type="wicri:Area/PubMed/Corpus">001218</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001218</idno><idno type="wicri:Area/PubMed/Curation">001218</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001218</idno><idno type="wicri:Area/PubMed/Checkpoint">000E80</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000E80</idno><idno type="wicri:Area/Ncbi/Merge">001522</idno><idno type="wicri:Area/Ncbi/Curation">001522</idno><idno type="wicri:Area/Ncbi/Checkpoint">001522</idno><idno type="wicri:Area/Main/Merge">001004</idno><idno type="wicri:Area/Main/Curation">001001</idno><idno type="wicri:Area/Main/Exploration">001001</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The Inhibitory Effect of Non-Substrate and Substrate DNA on the Ligation and Self-Adenylylation Reactions Catalyzed by T4 DNA Ligase</title><author><name sortKey="Bauer, Robert J" sort="Bauer, Robert J" uniqKey="Bauer R" first="Robert J." last="Bauer">Robert J. Bauer</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Evans, Thomas C" sort="Evans, Thomas C" uniqKey="Evans T" first="Thomas C." last="Evans">Thomas C. Evans</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Lohman, Gregory J S" sort="Lohman, Gregory J S" uniqKey="Lohman G" first="Gregory J. S." last="Lohman">Gregory J. S. Lohman</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalysis</term><term>DNA (chemistry)</term><term>DNA Ligases (chemistry)</term><term>DNA Replication</term><term>In Vitro Techniques</term><term>Kinetics</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN ()</term><term>Catalyse</term><term>Cinétique</term><term>DNA ligases ()</term><term>Réplication de l'ADN</term><term>Techniques in vitro</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA</term><term>DNA Ligases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>DNA Replication</term><term>In Vitro Techniques</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN</term><term>Catalyse</term><term>Cinétique</term><term>DNA ligases</term><term>Réplication de l'ADN</term><term>Techniques in vitro</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>DNA ligases are essential both to <italic>in vivo</italic> replication, repair and recombination processes, and <italic>in vitro</italic> molecular biology protocols. Prior characterization of DNA ligases through gel shift assays has shown the presence of a nick site to be essential for tight binding between the enzyme and its dsDNA substrate, with no interaction evident on dsDNA lacking a nick. In the current study, we observed a significant substrate inhibition effect, as well as the inhibition of both the self-adenylylation and nick-sealing steps of T4 DNA ligase by non-nicked, non-substrate dsDNA. Inhibition by non-substrate DNA was dependent only on the total DNA concentration rather than the structure; with 1 μg/mL of 40-mers, 75-mers, or circular plasmid DNA all inhibiting ligation equally. A >15-fold reduction in T4 DNA ligase self-adenylylation rate when in the presence of high non-nicked dsDNA concentrations was observed. Finally, EMSAs were utilized to demonstrate that non-substrate dsDNA can compete with nicked dsDNA substrates for enzyme binding. Based upon these data, we hypothesize the inhibition of T4 DNA ligase by non-nicked dsDNA is direct evidence for a two-step nick-binding mechanism, with an initial, nick-independent, transient dsDNA-binding event preceding a transition to a stable binding complex in the presence of a nick site.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Shuman, S" uniqKey="Shuman S">S Shuman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lehman, Ir" uniqKey="Lehman I">IR Lehman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cherepanov, Av" uniqKey="Cherepanov A">AV Cherepanov</name></author><author><name sortKey="De Vries, S" uniqKey="De Vries S">S de Vries</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Subramanya, Hs" uniqKey="Subramanya H">HS Subramanya</name></author><author><name sortKey="Doherty, Aj" uniqKey="Doherty A">AJ 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Bauer</name><name sortKey="Evans, Thomas C" sort="Evans, Thomas C" uniqKey="Evans T" first="Thomas C." last="Evans">Thomas C. Evans</name><name sortKey="Lohman, Gregory J S" sort="Lohman, Gregory J S" uniqKey="Lohman G" first="Gregory J. S." last="Lohman">Gregory J. S. Lohman</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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