Source:http://linkedlifedata.com/resource/pubmed/id/15763468
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2005-3-14
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pubmed:abstractText |
ZAM is an LTR-retrotransposon from Drosophila melanogaster that belongs to the genus errantivirus, viruses similar in structure and replication cycle to vertebrate retroviruses. A key component to its lifecycle is its reverse transcriptase which copies single-stranded genomic RNA into DNA. Here, we provide a detailed characterization of the enzymatic activities of the reverse transcriptase encoded by ZAM. When expressed in vitro, the reverse transcriptase domain associated with the RNase H domain encoded by the ZAM pol gene forms homodimers and displays an efficient RNA-dependent DNA-polymerase activity. It requires either Mg2+ or Mn2+ divalent cations, and works in basic pH, with a peak at around pH9. The so-called [RT-RH] polypeptide displays an optimal activity at 22 degrees C, a property that makes it well-adapted to the temperature of its host. This study contributes to our understanding of the general structures and functions of retroviral reverse transcriptases, a necessary process in the search for novel inhibitors.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0965-1748
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
323-31
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15763468-Animals,
pubmed-meshheading:15763468-Base Sequence,
pubmed-meshheading:15763468-Cloning, Molecular,
pubmed-meshheading:15763468-DNA,
pubmed-meshheading:15763468-DNA Primers,
pubmed-meshheading:15763468-Dimerization,
pubmed-meshheading:15763468-Drosophila melanogaster,
pubmed-meshheading:15763468-Kinetics,
pubmed-meshheading:15763468-RNA,
pubmed-meshheading:15763468-RNA-Directed DNA Polymerase,
pubmed-meshheading:15763468-Recombinant Fusion Proteins,
pubmed-meshheading:15763468-Retroviridae,
pubmed-meshheading:15763468-Thermodynamics
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pubmed:year |
2005
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pubmed:articleTitle |
Functional characteristics of a reverse transcriptase encoded by an endogenous retrovirus from Drosophila melanogaster.
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pubmed:affiliation |
INSERM U384, Faculty de Medecine, 28 Place Henri Dunant, 63000 Clermont-Ferrand, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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