Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13.
Identifieur interne : 002563 ( Main/Curation ); précédent : 002562; suivant : 002564Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13.
Auteurs : Na-Ra Lee [Corée du Sud] ; Hyun-Mi Kwon ; Kkothanahreum Park ; Sangtaek Oh ; Yong-Joo Jeong ; Dong-Eun KimSource :
- Nucleic acids research [ 1362-4962 ] ; 2010.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Virus du SRAS.
- métabolisme : ADN, Helicase, Protéines virales non structurales.
- ADN, Cinétique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : DNA.
- chemical , metabolism : DNA, DNA Helicases, Viral Nonstructural Proteins.
- enzymology : SARS Virus.
- Kinetics.
Abstract
SARS coronavirus encodes non-structural protein 13 (nsP13), a nucleic acid helicase/NTPase belonging to superfamily 1 helicase, which efficiently unwinds both partial-duplex RNA and DNA. In this study, unwinding of DNA substrates that had different duplex lengths and 5'-overhangs was examined under single-turnover reaction conditions in the presence of excess enzyme. The amount of DNA unwound decreased significantly as the length of the duplex increased, indicating a poor in vitro processivity. However, the quantity of duplex DNA unwound increased as the length of the single-stranded 5'-tail increased for the 50-bp duplex. This enhanced processivity was also observed for duplex DNA that had a longer single-stranded gap in between. These results demonstrate that nsP13 requires the presence of a long 5'-overhang to unwind longer DNA duplexes. In addition, enhanced DNA unwinding was observed for gapped DNA substrates that had a 5'-overhang, indicating that the translocated nsP13 molecules pile up and the preceding helicase facilitate DNA unwinding. Together with the propensity of oligomer formation of nsP13 molecules, we propose that the cooperative translocation by the functionally interacting oligomers of the helicase molecules loaded onto the 5'-overhang account for the observed enhanced processivity of DNA unwinding.
DOI: 10.1093/nar/gkq647
PubMed: 20671029
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pubmed:20671029Le document en format XML
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Park</name></author><author><name sortKey="Oh, Sangtaek" sort="Oh, Sangtaek" uniqKey="Oh S" first="Sangtaek" last="Oh">Sangtaek Oh</name></author><author><name sortKey="Jeong, Yong Joo" sort="Jeong, Yong Joo" uniqKey="Jeong Y" first="Yong-Joo" last="Jeong">Yong-Joo Jeong</name></author><author><name sortKey="Kim, Dong Eun" sort="Kim, Dong Eun" uniqKey="Kim D" first="Dong-Eun" last="Kim">Dong-Eun Kim</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20671029</idno><idno type="pmid">20671029</idno><idno type="doi">10.1093/nar/gkq647</idno><idno type="wicri:Area/PubMed/Corpus">001657</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001657</idno><idno type="wicri:Area/PubMed/Curation">001657</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001657</idno><idno type="wicri:Area/PubMed/Checkpoint">001697</idno><idno 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type="capital">Région capitale de Séoul</region></placeName></affiliation></author><author><name sortKey="Kwon, Hyun Mi" sort="Kwon, Hyun Mi" uniqKey="Kwon H" first="Hyun-Mi" last="Kwon">Hyun-Mi Kwon</name></author><author><name sortKey="Park, Kkothanahreum" sort="Park, Kkothanahreum" uniqKey="Park K" first="Kkothanahreum" last="Park">Kkothanahreum Park</name></author><author><name sortKey="Oh, Sangtaek" sort="Oh, Sangtaek" uniqKey="Oh S" first="Sangtaek" last="Oh">Sangtaek Oh</name></author><author><name sortKey="Jeong, Yong Joo" sort="Jeong, Yong Joo" uniqKey="Jeong Y" first="Yong-Joo" last="Jeong">Yong-Joo Jeong</name></author><author><name sortKey="Kim, Dong Eun" sort="Kim, Dong Eun" uniqKey="Kim D" first="Dong-Eun" last="Kim">Dong-Eun Kim</name></author></analytic><series><title level="j">Nucleic acids research</title><idno type="eISSN">1362-4962</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>DNA (chemistry)</term><term>DNA (metabolism)</term><term>DNA Helicases (metabolism)</term><term>Kinetics</term><term>SARS Virus (enzymology)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN ()</term><term>ADN (métabolisme)</term><term>Cinétique</term><term>Helicase (métabolisme)</term><term>Protéines virales non structurales (métabolisme)</term><term>Virus du SRAS (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA</term><term>DNA Helicases</term><term>Viral Nonstructural Proteins</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="métabolisme" xml:lang="fr"><term>ADN</term><term>Helicase</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN</term><term>Cinétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">SARS coronavirus encodes non-structural protein 13 (nsP13), a nucleic acid helicase/NTPase belonging to superfamily 1 helicase, which efficiently unwinds both partial-duplex RNA and DNA. In this study, unwinding of DNA substrates that had different duplex lengths and 5'-overhangs was examined under single-turnover reaction conditions in the presence of excess enzyme. The amount of DNA unwound decreased significantly as the length of the duplex increased, indicating a poor in vitro processivity. However, the quantity of duplex DNA unwound increased as the length of the single-stranded 5'-tail increased for the 50-bp duplex. This enhanced processivity was also observed for duplex DNA that had a longer single-stranded gap in between. These results demonstrate that nsP13 requires the presence of a long 5'-overhang to unwind longer DNA duplexes. In addition, enhanced DNA unwinding was observed for gapped DNA substrates that had a 5'-overhang, indicating that the translocated nsP13 molecules pile up and the preceding helicase facilitate DNA unwinding. Together with the propensity of oligomer formation of nsP13 molecules, we propose that the cooperative translocation by the functionally interacting oligomers of the helicase molecules loaded onto the 5'-overhang account for the observed enhanced processivity of DNA unwinding.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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