Drosophila signal peptide peptidase is an essential protease for larval development.
We identified the Drosophila melanogaster Signal peptide peptidase gene (Spp) that encodes a multipass transmembrane aspartyl protease. Drosophila SPP is homologous to the human signal peptide peptidase (SPP) and is distantly related to the presenilins. We show that, like human SPP, Drosophila SPP can proteolyze a model signal peptide and is sensitive to an SPP protease inhibitor and that it localizes to the endoplasmic reticulum. Expression of Drosophila SPP was first apparent at germ band extension, and in late embryos it was robust in the salivary glands, proventriculus, and tracheae. Flies bearing mutations in conserved residues or carrying deficiencies for the Spp gene had defective tracheae and died as larvae.
Casso
David J
DJ
Department of Biochemistry and Biophysics, University of California, San Francisco, 94143, USA.
Tanda
Soichi
S
Biehs
Brian
B
Martoglio
Bruno
B
Kornberg
Thomas B
TB
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000235:genetics / Q000502:physiology*; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D005455:Fluorescent Antibody Technique; D007814:Larva / Q000201:enzymology / Q000254:growth & development; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D014921:Wings, Animal / Q000201:enzymology / Q000254:growth & development
D016282:Aspartic Acid Endopeptidases; C460085:signal peptide peptidase
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