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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1996-7-23
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pubmed:abstractText |
The KP element can repress P element mobility in Drosophila melanogaster. Three mutant KP elements were made that had either two amino acid substitutions or a single amino acid deletion in the putative leucine zipper domain found in the KP polypeptide. Each KP element was expressed from the actin 5C proximal promoter. The wild-type control construct strongly repressed P element mobility, measured by the GD sterility and sn(w) mutability assays, in a position-independent manner. The single amino acid deletion mutant failed to repress P mobility by the double amino acid substitution mutants was position dependent. The results show that the leucine zipper of the KP polypeptide is important for P element regulation. This supports the multimer-poisoning model of P element repression, because leucine zipper motifs are involved in protein-protein interactions.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-115009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1311074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1313335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1333435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1645619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1648729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1653452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1655409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-16593888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1659442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1660427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1662417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-17248751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1849267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1852009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-1965103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2104658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2161558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2164887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2165865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2186528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2370661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2416475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2545526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2553268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2553270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2558959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2840331,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-2999793,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-3023899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-3289117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-553801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-6088058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-6289435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-6289436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-6309410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-8114699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-8224815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-8224830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-8290957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-8345525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8647395-8384145
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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 |
0016-6731
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
141
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
587-94
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8647395-Actins,
pubmed-meshheading:8647395-Amino Acid Sequence,
pubmed-meshheading:8647395-Animals,
pubmed-meshheading:8647395-Base Sequence,
pubmed-meshheading:8647395-DNA Primers,
pubmed-meshheading:8647395-DNA Transposable Elements,
pubmed-meshheading:8647395-Drosophila melanogaster,
pubmed-meshheading:8647395-Genetic Linkage,
pubmed-meshheading:8647395-Genotype,
pubmed-meshheading:8647395-Leucine Zippers,
pubmed-meshheading:8647395-Meiosis,
pubmed-meshheading:8647395-Molecular Sequence Data,
pubmed-meshheading:8647395-Mutagenesis,
pubmed-meshheading:8647395-Mutagenesis, Site-Directed,
pubmed-meshheading:8647395-Point Mutation,
pubmed-meshheading:8647395-Polymerase Chain Reaction,
pubmed-meshheading:8647395-Promoter Regions, Genetic,
pubmed-meshheading:8647395-Recombinant Fusion Proteins,
pubmed-meshheading:8647395-Recombination, Genetic,
pubmed-meshheading:8647395-Repressor Proteins,
pubmed-meshheading:8647395-Restriction Mapping
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pubmed:year |
1995
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pubmed:articleTitle |
A role for the KP leucine zipper in regulating P element transposition in Drosophila melanogaster.
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pubmed:affiliation |
Department of Biochemistry, University of Western Ontario, London, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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