pubmed-article:1310990 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1310990 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:1310990 | lifeskim:mentions | umls-concept:C0059946 | lld:lifeskim |
pubmed-article:1310990 | lifeskim:mentions | umls-concept:C1148735 | lld:lifeskim |
pubmed-article:1310990 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:1310990 | pubmed:dateCreated | 1992-3-24 | lld:pubmed |
pubmed-article:1310990 | 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. | lld:pubmed |
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pubmed-article:1310990 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1310990 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1310990 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1310990 | pubmed:month | Feb | lld:pubmed |
pubmed-article:1310990 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1310990 | pubmed:author | pubmed-author:Kowalczykowsk... | lld:pubmed |
pubmed-article:1310990 | pubmed:author | pubmed-author:RomanL JLJ | lld:pubmed |
pubmed-article:1310990 | pubmed:author | pubmed-author:EgglestonA... | lld:pubmed |
pubmed-article:1310990 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1310990 | pubmed:day | 25 | lld:pubmed |
pubmed-article:1310990 | pubmed:volume | 267 | lld:pubmed |
pubmed-article:1310990 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1310990 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1310990 | pubmed:pagination | 4207-14 | lld:pubmed |
pubmed-article:1310990 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1310990 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1310990 | pubmed:articleTitle | Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme. | lld:pubmed |
pubmed-article:1310990 | pubmed:affiliation | Department of Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611. | lld:pubmed |
pubmed-article:1310990 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1310990 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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