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Journal Article

Coexpression of two odorant-binding protein homologs in Drosophila: Implications for olfactory coding

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Steinbrecht,  Rudolf Alexander
Verhaltensphysiologie, Seewiesen, Max Planck Institut für Ornithologie, Max Planck Society;

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Citation

Hekmat-Scafe, D. S., Steinbrecht, R. A., & Carlson, J. R. (1997). Coexpression of two odorant-binding protein homologs in Drosophila: Implications for olfactory coding. The Journal of Neuroscience, 17(5), 1616-1624. doi:10.1523/JNEUROSCI.17-05-01616.1997.


Cite as: https://hdl.handle.net/21.11116/0000-000C-92ED-4
Abstract
Odorant-binding proteins (OBPs) are small soluble proteins present in the aqueous medium surrounding olfactory receptor neurons. Their function in olfaction is still unknown: they have been proposed to facilitate the transit of hydrophobic molecules to olfactory receptors, to deactivate the odorant stimulus, and/or to play a role in chemosensory coding. In this study we examine the genomic organization and expression patterns of two olfactory-specific genes (OS-E and OS-Fl of Drosophila melanogaster, the products of which are members of a protein family in Drosophila sharing sequence similarity with moth OBPs. We show that the OS-E and OS-F transcription units are located <1 kb apart. They are oriented in the same direction and display a similar intron-exon organization. Expression of both OS-E and OS-F proteins is restricted spatially to the ventrolateral region of the Drosophila antenna. Within this region both OS-E and OS-F proteins are expressed within two different types of sensory hairs: in most, if not all, sensilla trichodea and in similar to 40% of the interspersed small sensilla basiconica. We consistently observe that OS-E and OS-F are coexpressed, indicating that an individual sensillum can contain more than one odorant-binding protein. The functional significance of the observed expression pattern and its implications for olfactory coding are discussed.