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The Drosophila ninaE gene was isolated by a multistep protocol on the basis of its homology to bovine opsin cDNA. The gene encodes the major visual pigment protein (opsin) contained in Drosophila photoreceptor cells R1-R6. The coding sequence is interrupted by four short introns. The positions of three introns are conserved with respect to positions in mammalian opsin genes. The nucleotide sequence has intermittent regions of homology to bovine opsin coding sequences. The deduced amino acid sequence reveals significant homology to vertebrate opsins; there is strong conservation of the retinal binding site and two other regions. The predicted protein secondary structure strikingly resembles that of mammalian opsins. We conclude the Drosophila and vertebrate opsin genes are derived from a common ancestor.

The start sites of the araC and araBAD gene messenger of E. coli were located by transcription in vitro from short DNA fragments, by high magnification electron microscopy and by genetic mapping. Transcription for these messengers proceeds in opposite directions from the start sites that are 150 base pairs apart. Transcription from the araBAD promoter requires araC protein plus arabinose and CAP protein plus cyclic AMP. In the experiments performed in vitro, inducing the araBAD promoter represses activity of the araC promoter.

A 36 kilobase (kb) DNA segment of the Drosophila genome that contains several larval cuticle protein genes has been cloned and characterized. This segment maps at chromosomal locus 44D. It contains five genes, all of which are expressed at the same time of Drosophila development. Four of the genes are clustered within 7.9 kb of DNA and are abundantly expressed as poly(A) RNA in the epidermis of late third instar larvae but are not abundantly expressed in other developmental stages. A fifth gene lies 8 kb away from this cluster and is expressed at a much lower level in late third instar larval poly(A) RNA. Three of the four abundantly expressed genes have been shown to code for larval cuticle proteins; less decisive evidence indicates that the fourth gene also probably codes for a larval cuticle protein. Some of the genes are related in DNA sequence, and the proteins encoded in the cluster are related immunologically. Thus the cuticle genes encoded by the segment at 44D are members of a family of genes of common ancestry, which share the same pattern of developmental expression and reside in a small segment of the Drosophila genome.

The Drosophila dopa decarboxylase gene, Ddc, functions normally when reintroduced into flies. DNA containing a cloned Ddc gene inserted into a P element transposon was injected into early embryos. Transformants were identified by suppression of the cuticular phenotype of a Ddc mutant allele. The reintegrated genes are expressed in the proper tissue and at the proper stages during development even though their positions within the genome are different from that of the wild-type Ddc gene. Absolute levels of DDC enzyme activity are within 35% of that found in wild-type Canton S flies, the source of the transforming DNA. The transformants' Ddc RNA is indistinguishable from that of wild type. One reintegrated Ddc gene, inserted on the X chromosome, is affected by the dosage compensation mechanism that leads to sex-specific differences in the expression of many X-chromosome genes.