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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1992-3-24
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pubmed:abstractText |
A fluorescence assay was used to measure the processivity of Escherichia coli recBCD enzyme helicase activity. Under standard conditions, recBCD enzyme unwinds an average of 30 +/- 3.2 kilobase pairs (kb)/DNA end before dissociating. The average processivity (P obs) of DNA unwinding under these conditions is 0.99997, indicating that the probability of unwinding another base pair is 30,000-fold greater than the probability of dissociating from the double-stranded DNA. The average number of base pairs unwound per binding event (N) is sensitive to both mono- and divalent salt concentration and ranges from 36 kb at 80 mM NaCl to 15 kb at 280 mM NaCl. The processivity of unwinding increases in a hyperbolic manner with increasing ATP concentration, yielding a KN value for ATP of 41 +/- 9 microM and a limiting value of 32 +/- 1.8 kb/end for the number of base pairs unwound. The importance of the processivity of recBCD enzyme helicase activity to the recBCD enzyme-dependent stimulation of recombination at Chi sites observed in vivo is discussed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Monovalent,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonuclease V,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4207-14
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1310990-Adenosine Diphosphate,
pubmed-meshheading:1310990-Adenosine Triphosphate,
pubmed-meshheading:1310990-Cations, Divalent,
pubmed-meshheading:1310990-Cations, Monovalent,
pubmed-meshheading:1310990-DNA, Bacterial,
pubmed-meshheading:1310990-DNA Helicases,
pubmed-meshheading:1310990-Electrophoresis, Gel, Pulsed-Field,
pubmed-meshheading:1310990-Escherichia coli,
pubmed-meshheading:1310990-Exodeoxyribonuclease V,
pubmed-meshheading:1310990-Exodeoxyribonucleases,
pubmed-meshheading:1310990-Fluorescence Polarization
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pubmed:year |
1992
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pubmed:articleTitle |
Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme.
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pubmed:affiliation |
Department of Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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