| pubmed-article:8647395 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8647395 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8647395 | lifeskim:mentions | umls-concept:C0031705 | lld:lifeskim |
| pubmed-article:8647395 | lifeskim:mentions | umls-concept:C0040674 | lld:lifeskim |
| pubmed-article:8647395 | lifeskim:mentions | umls-concept:C0079686 | lld:lifeskim |
| pubmed-article:8647395 | lifeskim:mentions | umls-concept:C0013139 | lld:lifeskim |
| pubmed-article:8647395 | lifeskim:mentions | umls-concept:C1998811 | lld:lifeskim |
| pubmed-article:8647395 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8647395 | pubmed:dateCreated | 1996-7-23 | lld:pubmed |
| pubmed-article:8647395 | 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. | lld:pubmed |
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| pubmed-article:8647395 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8647395 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8647395 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8647395 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8647395 | pubmed:issn | 0016-6731 | lld:pubmed |
| pubmed-article:8647395 | pubmed:author | pubmed-author:AndrewsJ DJD | lld:pubmed |
| pubmed-article:8647395 | pubmed:author | pubmed-author:GloorG BGB | lld:pubmed |
| pubmed-article:8647395 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8647395 | pubmed:volume | 141 | lld:pubmed |
| pubmed-article:8647395 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8647395 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8647395 | pubmed:pagination | 587-94 | lld:pubmed |
| pubmed-article:8647395 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:8647395 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8647395 | pubmed:articleTitle | A role for the KP leucine zipper in regulating P element transposition in Drosophila melanogaster. | lld:pubmed |
| pubmed-article:8647395 | pubmed:affiliation | Department of Biochemistry, University of Western Ontario, London, Canada. | lld:pubmed |
| pubmed-article:8647395 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8647395 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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