In situ assay of light-stimulated G protein activity in Drosophila photoreceptor G protein beta mutants.
J Biol Chem
; 269(48): 30340-4, 1994 Dec 02.
Article
in En
| MEDLINE
| ID: mdl-7982946
ABSTRACT
An in situ 35S-labeled guanosine 5'-3-O-(thio)triphosphate (GTP gamma S) binding procedure was developed to assay light-stimulated G protein activity in Drosophila compound eyes. We found that Drosophila with mutations in G beta e, an abundant photoreceptor-specific G protein beta subunit essential for photoexcitation, are defective in light-stimulated [35S]GTP gamma S binding. We confirmed that G beta e interacts with a GTP-binding protein by demonstrating that immunoprecipitation of G beta e is sensitive to GTP gamma S. These results suggest that G beta e functions as the beta subunit of a heterotrimeric G protein that couples photoactivation of rhodopsin to downstream components in the Drosophila phototransduction cascade.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Guanosine 5'-O-(3-Thiotriphosphate)
/
Photoreceptor Cells, Invertebrate
/
GTP-Binding Proteins
/
Drosophila
Limits:
Animals
Language:
En
Journal:
J Biol Chem
Year:
1994
Document type:
Article