Cloning and characterization of αPS1, a novel Drosophila melanogaster integrin

Marcel Wehrli, Aaron DiAntonio, Ian M. Fearnley, Richard J. Smith, Michael Wilcox

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

The Drosophila position-specific integrins (PS integrins or PS antigens) comprise two heterodimeric complexes, αPS1βPS and αPS2βPS. With the cloning of αPS1 described here, we complete the characterization of the primary structure of the three PS integrin subunits. We have purified the αPS1 subunit, obtained peptide sequence and isolated genomic and cDNA clones. The encoded αPS1 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 αPS1 is distinct from all other alpha chains. The transcript analysis shows that the patterns of both αPS1 mRNA and protein expression are the same, suggesting that the gene is controlled transcriptionally. We compare the gene structures of the Drosophila αPS1, αPS2, the human αPS1and αPS2 (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.

Original languageEnglish
Pages (from-to)21-36
Number of pages16
JournalMechanisms of Development
Volume43
Issue number1
DOIs
StatePublished - Sep 1993

Keywords

  • Adhesion
  • Homology
  • Integrin
  • Intron
  • Molecular cloning

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