rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
18
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pubmed:dateCreated |
1992-10-22
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pubmed:abstractText |
In spite of the fact that a DNA helicase is clearly required for the predominantly leading-strand synthesis occurring during mammalian mtDNA replication, no such activity has heretofore been identified. We report the characterization of a mammalian mitochondrial DNA helicase isolated from bovine brain tissue. The sucrose gradient-purified mitochondria in which the activity was detected had less than 1 part in 2500 nuclear contamination according to Western blot analysis using nuclear- and mitochondrial-specific probes. Mitochondrial protein fractionation by DEAE-Sephacel chromatography yielded a DNA helicase activity dependent upon hydrolysis of ATP or dATP but not other NTPs or dNTPs. The mitochondrial helicase unwound 15- and 20-base oligonucleotides but was unable to unwind 32-base or longer oligonucleotides, and the polarity of the unwinding is 3'-to-5' with respect to the single-stranded portion of the partial duplex DNA substrate. This direction of unwinding would place the bovine mitochondrial helicase on the template strand ahead of DNA polymerase gamma during mtDNA replication, a situation analogous to that of the Rep helicase of Escherichia coli during leading-strand DNA synthesis of certain bacteriophages.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1326759-1064029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1326759-1176550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1326759-138139,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1326759-2461720,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1326759-6978464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1326759-7120390
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
89
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
8562-6
|
pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1326759-Adenosine Triphosphate,
pubmed-meshheading:1326759-Animals,
pubmed-meshheading:1326759-Base Sequence,
pubmed-meshheading:1326759-Brain,
pubmed-meshheading:1326759-Cattle,
pubmed-meshheading:1326759-Cell Fractionation,
pubmed-meshheading:1326759-DNA, Mitochondrial,
pubmed-meshheading:1326759-DNA Helicases,
pubmed-meshheading:1326759-DNA Replication,
pubmed-meshheading:1326759-Deoxyadenine Nucleotides,
pubmed-meshheading:1326759-Mitochondria,
pubmed-meshheading:1326759-Molecular Sequence Data,
pubmed-meshheading:1326759-Oligodeoxyribonucleotides,
pubmed-meshheading:1326759-Substrate Specificity
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pubmed:year |
1992
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pubmed:articleTitle |
DNA helicase from mammalian mitochondria.
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pubmed:affiliation |
Department of Immunology, University of Florida, Gainesville 32610.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|