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Genetics, Vol 141, 587-594, Copyright © 1995
INVESTIGATIONS |
A Role for the KP Leucine Zipper in Regulating P Element Transposition in Drosophila melanogaster
J. D. Andrews and G. B. Gloor
Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1
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 regardless of its insertion site, while repression of P element 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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