An opsin gene that is expressed only in the R7 photoreceptor cell of Drosophila

• Published in: The EMBO journal Vol. 6; no. 2; pp. 443 - 451
• Main Authors: Fryxell, K.J., Meyerowitz, E.M.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 01-02-1987
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Cloning, Molecular; Drosophila melanogaster; Drosophila melanogaster - genetics; Drosophilidae; Eye Proteins - genetics; Fundamental and applied biological sciences. Psychology; Gene expression; Genes; Molecular and cellular biology; Molecular genetics; nucleotide sequence; opsin; Photoreceptor Cells - metabolism; photoreceptors; Retinal Pigments - genetics; Rod Opsins; Transcription, Genetic; Eye; Regulation(control); Arthropoda; Animal; Insecta; Tissue specificity; Opsin; Invertebrata; Gene expression; Drosophila melanogaster
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1987.tb04774.x

We have used two techniques to isolate and characterize eye‐specific genes from Drosophila melanogaster. First, we identified genes whose expression is limited to eyes, photoreceptor cells, or R7 photoreceptor cells by differential screening with [32P]cDNAs derived from the heads of mutant flies that have reduced amounts of these tissues and cells (Microcephalus, glass3, and sevenless, respectively). Secondly, we identified opsin genes by hybridization with synthetic [32P]oligonucleotides that encode domains that have been conserved between some opsin genes. We found seven clones that contain genes expressed only in the eye or optic lobes of Drosophila; three are expressed only in photoreceptor cells. One is expressed only in R7 photoreceptor cells and hybridizes to some of the previously mentioned oligonucleotides. The complete DNA sequence of the R7‐specific opsin gene and its 5′ and 3′ flanking regions was determined. It is quite different from other known Drosophila opsin genes, in that it is not interrupted by introns and shares only 37‐38% amino acid identity with the proteins encoded by these genes. The predicted protein structure contains many characteristics that are common to all rhodopsins, and the sequence differences help to identify four domains of the rhodopsin molecule that have been conserved in evolution.