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Sex pheromone receptor proteins. Visualization using a radiolabeled photoaffinity analog
R G Vogt1, G D Prestwich, L M Riddiford
1Department of Chemistry, State University of New York, Stony Brook 11794-3400.
The Journal of Biological Chemistry
|March 15, 1988
Summary
Researchers used a labeled pheromone analog to identify proteins in moth antennae that bind to odorants. This study provides direct evidence of a membrane protein interacting with a specific odorant in a chemosensory neuron.
Area of Science:
- Chemical Ecology
- Neurobiology
- Molecular Biology
Background:
- Moth olfaction relies on specific pheromone-binding proteins.
- The precise molecular interactions in chemosensory neurons remain incompletely understood.
Purpose of the Study:
- To directly identify and characterize pheromone-binding proteins in the male silk moth, Antheraea polyphemus.
- To provide evidence for the interaction of membrane proteins with odorants in chemosensory neurons.
Main Methods:
- Utilized a tritium-labeled photoaffinity analog of moth pheromone, (E,Z)-6,11-[3H]hexadecadienyl diazoacetate.
- Employed fluorescence autoradiography of electrophoretically separated antennal proteins.
- Assessed specificity by competition with unlabeled pheromone, (E,Z)-6,11-hexadecadienyl acetate.
Main Results:
- Covalently modified and visualized a 15-kilodalton soluble protein and a 69-kilodalton membrane protein.
- Demonstrated specific covalent modification, which was reduced by excess unlabeled pheromone.
- Identified a membrane-bound protein interacting with the pheromone analog.
Conclusions:
- This study provides the first direct evidence for a membrane protein on a chemosensory neuron specifically interacting with a biologically relevant odorant.
- The identified proteins are likely involved in pheromone detection and signal transduction in Antheraea polyphemus.