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Oligomerization of the human delta-opioid receptor and its regulation by ligand occupancy were explored following expression in HEK293 cells using each of co-immunoprecipitation of differentially epitope-tagged forms of the receptor, bioluminescence resonance energy transfer and time-resolved fluorescence resonance energy transfer. All of the approaches identified constitutively formed receptor oligomers, and the time-resolved fluorescence studies confirmed the presence of such homo-oligomers at the cell surface. Neither the agonist ligand [d-Ala(2),d-Leu(5)]enkephalin nor the inverse agonist ligand ICI174864 were able to modulate the oligomerization status of this receptor. Interactions between co-expressed delta-opioid receptors and beta(2)-adrenoreceptors were observed in co-immunoprecipitation studies. Such hetero-oligomers could also be detected using bioluminescence resonance energy transfer although the signal obtained was substantially smaller than for homo-oligomers of either receptor type. Signal corresponding to the delta-opioid receptor-beta(2)-adrenoreceptor hetero-oligomer was increased in the presence of agonist for either receptor. However, substantial levels of this hetero-oligomer were not detected at the cell surface using time-resolved fluorescence resonance energy transfer. These studies demonstrate that, following transient transfection of HEK293 cells, constitutively formed oligomers of the human delta-opioid receptor can be detected by a variety of approaches. However, these are not regulated by ligand occupancy. They also indicate that time-resolved fluorescence resonance energy transfer represents a means to detect such oligomers at the cell surface in populations of intact cells.

I-R hybrid dysgenesis in D. melanogaster is controlled by transposable elements known as I factors. We have determined the base sequences of one complete I factor and the ends of six others. The ends of these elements are highly conserved and are flanked by target site duplications varying in length from 10–14 bp. There are no terminal repeats, and the 3′ end of one strand is A-rich, having 4–7 tandem repeats of the sequence TAA. This sequence organization is similar to that of mammalian LINEs, or L1 elements. The complete I factor sequence contains two long open reading frames, ORF1 and ORF2, of 1278 and 3258 bp. ORF1 encodes a possible nucleic acid-binding protein, and part of the amino acid sequence of ORF2 is similar to that of viral reverse transcriptases and polypeptides encoded by L1 elements. These results suggest that I factors transpose by reverse transcription of a full-length RNA.