Cooperative Activity of SARS Coronavirus Nsp13 Helicase Characterized by Single Molecule FRET
Identifieur interne : 000770 ( Pmc/Corpus ); précédent : 000769; suivant : 000771Cooperative Activity of SARS Coronavirus Nsp13 Helicase Characterized by Single Molecule FRET
Auteurs : Hyeryeon Im ; Sangmi Jee ; Gwangrog LeeSource :
- Biophysical Journal [ 0006-3495 ] ; 2015.
Url:
DOI: 10.1016/j.bpj.2014.11.426
PubMed: NONE
PubMed Central: 7111059
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Cooperative Activity of SARS Coronavirus Nsp13 Helicase Characterized by Single Molecule FRET</title><author><name sortKey="Im, Hyeryeon" sort="Im, Hyeryeon" uniqKey="Im H" first="Hyeryeon" last="Im">Hyeryeon Im</name></author><author><name sortKey="Jee, Sangmi" sort="Jee, Sangmi" uniqKey="Jee S" first="Sangmi" last="Jee">Sangmi Jee</name></author><author><name sortKey="Lee, Gwangrog" sort="Lee, Gwangrog" uniqKey="Lee G" first="Gwangrog" last="Lee">Gwangrog Lee</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmc">7111059</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111059</idno><idno type="RBID">PMC:7111059</idno><idno type="doi">10.1016/j.bpj.2014.11.426</idno><idno type="pmid">NONE</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">000770</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000770</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Cooperative Activity of SARS Coronavirus Nsp13 Helicase Characterized by Single Molecule FRET</title><author><name sortKey="Im, Hyeryeon" sort="Im, Hyeryeon" uniqKey="Im H" first="Hyeryeon" last="Im">Hyeryeon Im</name></author><author><name sortKey="Jee, Sangmi" sort="Jee, Sangmi" uniqKey="Jee S" first="Sangmi" last="Jee">Sangmi Jee</name></author><author><name sortKey="Lee, Gwangrog" sort="Lee, Gwangrog" uniqKey="Lee G" first="Gwangrog" last="Lee">Gwangrog Lee</name></author></analytic><series><title level="j">Biophysical Journal</title><idno type="ISSN">0006-3495</idno><idno type="eISSN">1542-0086</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader></TEI><pmc article-type="abstract"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Biophys J</journal-id><journal-id journal-id-type="iso-abbrev">Biophys. J</journal-id><journal-title-group><journal-title>Biophysical Journal</journal-title></journal-title-group><issn pub-type="ppub">0006-3495</issn><issn pub-type="epub">1542-0086</issn><publisher><publisher-name>Biophysical Society. Published by Elsevier Inc.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmc">7111059</article-id><article-id pub-id-type="publisher-id">S0006-3495(14)01635-X</article-id><article-id pub-id-type="doi">10.1016/j.bpj.2014.11.426</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Cooperative Activity of SARS Coronavirus Nsp13 Helicase Characterized by Single Molecule FRET</article-title></title-group><contrib-group><contrib contrib-type="author" id="au1"><name><surname>Im</surname><given-names>Hyeryeon</given-names></name></contrib><contrib contrib-type="author" id="au2"><name><surname>Jee</surname><given-names>Sangmi</given-names></name></contrib><contrib contrib-type="author" id="au3"><name><surname>Lee</surname><given-names>Gwangrog</given-names></name></contrib></contrib-group><aff id="aff1">Life Science, Gwangju Institute of Science and Technology, Gwangju, Korea, Republic of</aff><pub-date pub-type="pmc-release"><day>27</day><month>1</month><year>2015</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><day>27</day><month>1</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>27</day><month>1</month><year>2015</year></pub-date><volume>108</volume><issue>2</issue><fpage>72a</fpage><lpage>72a</lpage><permissions><copyright-statement>Copyright © 2015 Biophysical Society. Published by Elsevier Inc.</copyright-statement><copyright-year>2015</copyright-year><copyright-holder>Biophysical Society</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions></article-meta><notes><p id="misc0010">363-Pos B143</p></notes></front><body><p id="p0010">SARS was epidemic in 2003 worldwide. SARS-CoV helicase plays critical roles in viral replication, and has been proposed to be a potential candidate for anti-SARS therapy. We use single molecule fluorescence resonance energy transfer to examine the unwinding and rewinding mechanism of nsP13 helicase on partial DNA duplexes as a function of protein, ATP concentration, and tail length. Our results reveal that the tail length of the substrates determines the total amount of DNA unwound by increasing the number of proteins loaded. In contrast, unwinding rate and step size increase as a function of the protein and ATP concentration for the partial duplex with a long tail (45nts long), but independent of protein concentration for the short tail (30nts long). We also observed a repetitive unwinding displaying multiple rounds of re-unwinding and re-zipping events where re-unwinding becomes favorable at higher protein concentration. We also found that the relative extent of constitutive unwinding and repetitive fluctuation is defined by the modality of DNA-Protein complex in the presence or absence of ATP concentration. The ratio between them determines the processivity of the cooperative helicases in tandem. In general, our results identify the important cellular parameters, governing the cooperative unwinding and repetitive rewinding behavior of helicase. This is a new attempt to understand the complicate behavior of unwinding motor cohorts at the single molecule resolution.</p></body></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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