Abstract
Using oligonucleotide probes derived from consensus sequences for glycoprotein hormone receptors, we have cloned an 831-amino acid residue-long receptor from Drosophila melanogaster that shows a striking structural homology with members of the glycoprotein hormone (thyroid-stimulating hormone (TSH); follicle-stimulating hormone (FSH); luteinizing hormone/choriogonadotropin (LH/CG)) receptor family from mammals. This homology includes a very large, extracellular N terminus (20% sequence identity with rat TSH, 19% with rat FSH, and 20% with the rat LH/CG receptor) and a seven-transmembrane region (53% sequence identity with rat TSH, 50% with rat FSH, and 52% with the rat LH/CG receptor). The Drosophila receptor gene is >7.5 kilobase pairs long and contains 17 exons and 16 introns. Seven intron positions coincide with introns in the mammalian glycoprotein hormone receptor genes and have the same intron phasing. This indicates that the Drosophila receptor is evolutionarily related to the mammalian receptors. The Drosophila receptor gene is located at position 90C on the right arm of the third chromosome. The receptor is strongly expressed starting 8-16 h after oviposition, and the expression stays high until after pupation. Adult male flies express high levels of receptor mRNA, but female flies express about 6 times less. The expression pattern in embryos and larvae suggests that the receptor is involved in insect development. This is the first report on the molecular cloning of a glycoprotein hormone receptor family member from insects.
Highlights
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) U47005, U47006, and U49733
Using the polymerase chain reaction (PCR) and primers coding for consensus sequences of G protein-coupled receptors, we have found that cnidarians produce a receptor that shows a striking structural homology with members of the mammalian thyroidstimulating hormone (TSH), follicle-stimulating hormone (FSH), luteinizing hormone/ choriogonadotropin (LH/CG) receptors [14]
CDNA Cloning of a Drosophila Receptor Protein—We constructed one sense PCR primer that was based on conserved amino acid sequences located N-terminally of the first membrane-spanning domain of several mammalian glycoprotein hormone receptors and a second antisense primer corresponding to conserved amino acid sequences of the second membrane-spanning region
Summary
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) U47005, U47006, and U49733. Using the polymerase chain reaction (PCR) and primers coding for consensus sequences of G protein-coupled receptors, we have found that cnidarians (which are the most primitive animals in the animal kingdom having a nervous system, such as sea anemones) produce a receptor that shows a striking structural homology with members of the mammalian TSH, FSH, LH/CG receptors [14]. This was an exciting finding, since glycoprotein hormone receptors had, so far, only been cloned from mammals and not from other vertebrates or invertebrates. Present paper, we have focused on insects, and we have cloned and characterized a Drosophila melanogaster receptor that shows a strong, structural homology with the TSH, FSH, LH/CG receptors from mammals
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