Cloning and characterization of αPS1, a novel Drosophila melanogaster integrin

Abstract

The Drosophila position-specific integrins (PS integrins or PS antigens) comprise two heterodimeric complexes, α PS1 β PS and α PS2 β PS. With the cloning of α PS1 described here, we complete the characterization of the primary structure of the three PS integrin subunits. We have purified the α PS1 subunit, obtained peptide sequence and isolated genomic and cDNA clones. The encoded α PS1 protein contains pattern of the cleaved alpha integrins, three putative metal binding domains and shows the other characteristic features of alpha integrins. Regions of sequence variation indicate that α PS1 is distinct from all other alpha chains. The transcript analysis shows that the patterns of both α PS1 mRNA and protein expression are the same, suggesting that the gene is controlled transcriptionally. We compare the gene structures of the Drosophila α PS1, α PS2, the human α PS1and α PS2 (p150,95) and the C. elegans F54G8.3 integrins. We find several positions and phases of introns conserved which, supported by conservation also in the amino acid sequence, indicates that they all derive from a common ancestral gene.