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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
1993-11-10
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pubmed:abstractText |
We have purified a DNA polymerase activity from 0- to 2-hr embryos of Drosophila melanogaster to near homogeneity. The purified enzyme consists of a single 120-kDa polypeptide, which contains polymerase and 3'-->5' exonuclease activities. Exonuclease activity is inhibited by deoxynucleoside triphosphates, suggesting that the polymerase and exonuclease activities are coupled. The polymerase is more active with poly(dA-dT) than with activated DNA or poly(dA)/oligo(dT) as template. It shows a low degree of processivity with poly(dA)/oligo(dT). The polymerase is sensitive to aphidicolin and carbonyldiphosphonate but resistant to N2-[p-(n-butyl)phenyl]-2-deoxyguanosine triphosphate, 2-[p-(n-butyl)anilino]-2-deoxyadenosine triphosphate, and dideoxythymidine triphosphate. The 120-kDa polypeptide can be distinguished from the large subunit of Drosophila DNA polymerase alpha on the basis of the peptides generated by partial cleavage with N-chlorosuccinimide and by its failure to react with a monoclonal antibody directed against the large subunit of DNA polymerase alpha. The DNA polymerase is inhibited by 200 mM NaCl and is unable to use poly(rA)/oligo(dT) as a template, thus differentiating it from DNA polymerase gamma. On the basis of these properties, we propose that the DNA polymerase that we have purified from 0- to 2-hr Drosophila melanogaster embryos is DNA polymerase delta.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1348971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1360647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1429661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1674744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1682322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1682323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1704371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1727692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1846563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1883203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1973166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1975694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-1975812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-2169349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-2505329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-2527747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-2882423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-2882424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-2902631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-3031067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-3112771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-3277667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-3289619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-3745189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-4208784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-4859478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-6187241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-6403945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-7304986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-8423775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-8494903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8415662-942051
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9105-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8415662-Animals,
pubmed-meshheading:8415662-Chromatography,
pubmed-meshheading:8415662-Chromatography, Affinity,
pubmed-meshheading:8415662-Chromatography, Ion Exchange,
pubmed-meshheading:8415662-DNA Polymerase III,
pubmed-meshheading:8415662-DNA-Directed DNA Polymerase,
pubmed-meshheading:8415662-Drosophila melanogaster,
pubmed-meshheading:8415662-Durapatite,
pubmed-meshheading:8415662-Embryo, Nonmammalian,
pubmed-meshheading:8415662-Kinetics,
pubmed-meshheading:8415662-Macromolecular Substances,
pubmed-meshheading:8415662-Molecular Weight,
pubmed-meshheading:8415662-Peptide Mapping
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pubmed:year |
1993
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pubmed:articleTitle |
DNA polymerase delta from embryos of Drosophila melanogaster.
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pubmed:affiliation |
Department of Biochemistry, Beckman Center, Stanford University, CA 94305.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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