rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
50
|
pubmed:dateCreated |
2007-12-13
|
pubmed:abstractText |
Helicases are enzymes that couple ATP hydrolysis to the unwinding of double-stranded (ds) nucleic acids. The bacteriophage T4 helicase (gp41) is a hexameric helicase that promotes DNA replication within a highly coordinated protein complex termed the replisome. Despite recent progress, the gp41 unwinding mechanism and regulatory interactions within the replisome remain unclear. Here we use a single tethered DNA hairpin as a real-time reporter of gp41-mediated dsDNA unwinding and single-stranded (ss) DNA translocation with 3-base pair (bp) resolution. Although gp41 translocates on ssDNA as fast as the in vivo replication fork ( approximately 400 bp/s), its unwinding rate extrapolated to zero force is much slower ( approximately 30 bp/s). Together, our results have two implications: first, gp41 unwinds DNA through a passive mechanism; second, this weak helicase cannot efficiently unwind the T4 genome alone. Our results suggest that important regulations occur within the replisome to achieve rapid and processive replication.
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pubmed:grant |
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-10899133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-10966472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-11207360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-11395406,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-12574500,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-15079074,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-8811178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-8962073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-9342340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18077411-9671724
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
1091-6490
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
11
|
pubmed:volume |
104
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
19790-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2007
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pubmed:articleTitle |
Real-time observation of bacteriophage T4 gp41 helicase reveals an unwinding mechanism.
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pubmed:affiliation |
Laboratoire de Physique Statistique, Ecole Normale Supérieure, Centre National de la Recherche Scientifique-UMR8550, 24 Rue Lhomond, 75005 Paris, France. tlionnet@aecom.yu.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|